The Protein Family of RNA Helicases

References

• Abramson, R. D., Dever, T. E., Lawson, T. G., Ray, B. K., Thach, R. E., and Merrick, W. C. (1987). The ATP-dependent interaction of eukaryotic initiation factors with mRNA. J. Biol. Chem. 262: 3826—3832.
   PubMedGoogle Scholar
• Abramson, R. D., Dever, T. E., and Merrick, W. C. (1988). Biochemical evidence supporting a mechanism for cap-independent and internal initiation of eukaryotic mRNA. J. Biol. Chem. 263: 6016—6019.
   PubMedGoogle Scholar
• Altamura, N., Dujardin, G., Groudinsky, O., and Slonimski, P. P. (1994). Two adjacent nuclear genes, ISF1 and NAM7/UPF1, cooperately participate in mitochondrial functions in Sac- charomyces cerevisiae. Mol. <i>Gen. Genet. 242: 49—56.
   Google Scholar
• Altamura, N., Groudinsky, O., Dujardin, G., and Slonimski, P. P. (1992). NAM7 nuclear gene encodes a novel member of a family of heli- cases with a Zn-ligand motif and is involved in mitochondrial functions in Saccharomyces cerevisiae. J. <i>Mol. Biol. 224: 575—587.
   Google Scholar
• Altmann, M., Muller, P. P., Wittmer, B., Ruchti, F., Lanker, S., and Trachsel, H. (1993). A Saccharomyces cerevsiae homologue of mammalian translation initiation factor eIF-4B contributes to RNA helicase activity. EMBO J. 12: 3997—4003.
   PubMed Web of Science ®Google Scholar
• Altmann, M., Schmitz, N., Berset, C., and Trachsel, H. (1997). A novel inhibitor of cap-dependent translation initiation in yeast: p20 competes with eIF4G for binding to eIF4E. EMBO J. 16: 1114—1121.
   PubMed Web of Science ®Google Scholar
• Arenas, J. E. and Abelson, J. N. (1997). Prp43: An RNA helicase-like factor involved in spliceo- some disassembly. Proc. Natl. Acad. Sci. USA 94: 11798—11802.
   PubMed Web of Science ®Google Scholar
• Bayliss, C. and Condits, R. C. (1996). The vaccinia virus A18R gene product is a DNA-dependent ATPase. J. Biol. Chem. 270: 1550—1556.
   Google Scholar
• Ben Asher, E., Groudinsky, O., Dujardin, G., Altamura, N., Kermorgant, M., and Slonimski, P. P. (1989). Novel class of nuclear genes involved in both mRNA splicing and protein synthesis in S. cerevisiae mitochondria. Mol. Gen. Genet:. 215: 517—528.
   Google Scholar
• Blum, S., Mueller, M., Schmid, S. R., Linder, P., and Trachsel, H. (1989). Translation in Saccha- romyces cerevisiae: initiation factor 4A-depen- dent cell-free system. Proc. Natl. Acad. Sci. USA 86: 6043—6046.
   PubMed Web of Science ®Google Scholar
• Boddeker, N., Stade, K., and Franceschi, F. (1997). Characterization of DbpA, an Escherichia coli DEAD box protein with ATP-independent RNA unwinding activity. Nucleic Acids Res. 25: 537—545.
   PubMedGoogle Scholar
• Brockdorff, N., Ashworth, A., Kay, G. F., McCabe, V. M., Norris, D. P. C., P. J., Swift, S., and Rastan, S. (1992). The product of the mouse Xist gene is a 15 kb inactive X-specific transcript containing no conserved ORF and located in the nucleus. Cell 71: 515—526.
   PubMed Web of Science ®Google Scholar
• Brown, C. J., Henddrich, B. D., Rupert, J. L., Lafreniere, R. G., Xing, Y., Lawrence, J., and Willard, H. F. (1992). The human XIST gene: analysis of a 17-kb inactive X-specific RNA that contains conserved repeats and is highly localized within the nucleus. Cell 71: 527—542.
   PubMed Web of Science ®Google Scholar
• Broyles, S. S. and Moss, B. (1987). Identification of the vaccinia virus gene encoding nucleo- side triphosphate phosphohydrolase I, a DNA- dependent ATPase. J. Virology61: 1738—1742.
   Google Scholar
• Buelt, M. K., Glidden, B. J., and Storm, D. R. (1994). Regulation of p68 RNA helicase by Calmudin and protein kinase C. J. Biol. Chem. 269: 29367—29370.
   PubMedGoogle Scholar
• Burke, J. M. (1988). Molecular genetics of group I introns, RNA structures and protein factors required for splicing — a review. Gene 73: 273294.
   Google Scholar
• Chang, T.-H., Arenas, J., and Abelson, J. (1990). Identification of five putative RNA helicase genes. Proc. Natl. Acad. Sci. USA 87: 15711575.
   Google Scholar
• Cheng, J., Fogel-Petrovic, M., and Maquat, L. E. (1990). Translation to near the distal end of the penultimate exon is required for normal levels of spliced triosephosphate isomerase mRNA. Mol. Cell. Biol. 10: 5215—5225.
   PubMedGoogle Scholar
• Chuang, R.-Y., Weaver, P. L., Liu, Z., and Chang, T.-H. (1997). Requirement of the DEAD-box protein Ded1p for messenger RNA translation. Science 275: 1468—1471.
   PubMed Web of Science ®Google Scholar
• Claude, A., Arenas, J. E., and Hurwitz, J. (1991). The isolation and characterization of a RNA helicase from nuclear extracts of HeLa cells. J. Biol. Chem. 266: 10358—10367.
   Google Scholar
• Company, M., Arenas, J., and Abelson, J. (1991). Requirement of the RNA helicase-like protein PRP22 for release of messenger RNA from spliceosomes. Nature 349: 487—493.
   PubMed Web of Science ®Google Scholar
• Conrad-Webb, H., Perlman, P. S., Zhu, H., and Butow, R. A. (1990). The nuclear SUV3—1 mutation affects a variety of post-transcriptional processes in yeast mitochondria. Nucleic Acids Res. 18: 1369—1376.
   Google Scholar
• Conroy, S. C., Dever, T. E., Owens, C. L., and Merrick, W. C. (1990). Characterization of the 46,000 dalton subunit of the eIF-4A. Arch. Bio- chem. Biophys. 282: 363—371.
   PubMedGoogle Scholar
• Czaplinski, K., Weng, Y., Hagan, K. W., and Peltz, S. W. (1995). Purification and characterization of the Upf1 protein: a factor involved in translation and mRNA degradation. RNA 1: 610623.
   Google Scholar
• Dalbadie-McFarland, G. and Abelson, J. N. (1990). A helicase-like protein required for mRNA splicing in yeast. Proc. Natl. Acad. Sci. USA 87: 4263—4240.
   Google Scholar
• Daugeron, M. C. and Linder, P. (1998). Dbp7p, a putative ATP-dependent RNA helicase from Saccharomyces cerevisiae, is required for 60S ribosomal subunit assembly. RNA 4: 566—581.
   PubMed Web of Science ®Google Scholar
• de la Cruz, J., Iost, I., Kressler, D., and Linder, P. (1997). The p20 and Ded1 proteins have antagonistic roles in eIF4E-dependent translation in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 94: 5201—5206.
   PubMed Web of Science ®Google Scholar
• de la Cruz, J., Kressler, D., Tollervey, D., and Linder, P. (1998). Dob1p (Mtr4p) is a putative ATP-dependent RNA helicase required for the 3' end formation of 5.8S rRNA in Saccharomyces cerevisiae. EMBO J. 17: 11281140.
   Google Scholar
• de Valoir, T., Tucker, M. A., Belikoff, E. J., Camp, L. A., Bolduc, C., and Beckingham, K. (1991). A second maternally expressed Drosophila gene encodes a putative RNA helicase of the “DEAD box” family. Proc. Natl. Acad. Sci. USA 88: 2113—2117.
   PubMedGoogle Scholar
• Dmochowska, A., Golik, P., and Stepien, P. (1995). The novel nuclear gene DSS-1 of Saccharomy- ces cerevisiae is necessary for mitochondrial biogenesis. Curr. Genet. 28: 108—112.
   PubMed Web of Science ®Google Scholar
• Dykstra, C. C., Kitada, K., Clark, A. B., Hamataka, R. K., and Sugino, A. (1991). Cloning and characterizing of DST2, the gene for DNA strand transfer protein b from Saccharomyces cerevi- siae. Mol. Cell. Biol. 11: 2583—2592.
   Google Scholar
• Eichler, D. C. and Craig, N. (1994). Processing of eukaryotic ribosomal RNA. Prog. Nucleic Acids Res. Mol. Biol. 49: 197—239.
   PubMedGoogle Scholar
• Fathi, Z. and Condit, R. C. (1991a). Genetic and molecular biological characterization of a vaccinia virus temperature-sensitve complementation group affecting a virion component. Virology 181: 258—272.
   PubMed Web of Science ®Google Scholar
• Fathi, Z. and Condit, R. C. (1991b). Phenotypic characterization of a vaccinia virus temperatur- sensitive complementation group affecting a virion component. Virology 181: 273—276.
   PubMed Web of Science ®Google Scholar
• Fernandez, A., Lain, S., and Garcia, A. (1995). RNA helicase activity of the plum pox potyvirus CI protein expressed in Escherichia coli. Mapping of an RNA binding domain. Nucleic Acids Res. 23: 1327—1332.
   PubMedGoogle Scholar
• Flores-Rozas, H. and Hurwitz, J. (1993). Characterization of a new RNA helicase from nuclear extracts of Hela cells which translocates in the 5' to 3' direction. J. Biol. Chem. 268: 2137221383.
   Google Scholar
• Ford, M. J., Anton, I. A., and Lane, D. P. (1988). Nuclear protein with sequence homology to translation initiation factor eIF-4A. Nature 322: 736—738.
   Google Scholar
• Fornerod, M., Ohno, M., Yoshida, M., and Mattaj, I. W. (1997). CRM1 is an export receptor for leucine-rich nuclear export signals. Cell 90: 1051—1060.
   PubMed Web of Science ®Google Scholar
• Fry, D. C., Kuby, S. A., and Mildvan, A. S. (1986). ATP-binding site of adenylate kinase: mechanistic implications of its homology with ras- encoded p21, Fj-ATPase, and other nucleotide- binding proteins. Proc. Natl. Acad. Sci. USA 83: 907—911.
   PubMed Web of Science ®Google Scholar
• Fuller-Pace, F. V. (1994). RNA helicases: modulators of RNA structure. Trends Cell Biol. 4: 271—274.
   PubMedGoogle Scholar
• Fuller-Pace, F. V., Nicol, S. M., Reid, A. D., and Lane, D. P. (1993). DbpA; a DEAD box protein specifically activated by 23S rRNA. EMBO J. 12: 3619—3626.
   PubMedGoogle Scholar
• Gershon, P. D. and Moss, B. (1990). Early transcription factor subunits are encoding by vaccinia virus late genes. Proc. Natl. Acad. Sci. USA 87: 4401—4405.
   PubMedGoogle Scholar
• Golubovsky, M. D. and Ivanov, Y. N. (1972). Autosomal mutation in Drosophila melanogas- ter killing the males and connected with female sterility. Dros. Info. Serv. 49: 117.
   Google Scholar
• Gorbalenya, A. E. and Koonin, E. V. (1989). Viral proteins containing the purine NTP-binding sequence pattern. Nucleic Acids Res. 17: 84138440.
   Google Scholar
• Gorbalenya, A. E. and Koonin, E. Y. (1991). Endo- nuclease (R) subunit of type-I and type-III restriction modification enzymes contain a he- licase-like domain. FEBS Lett. 291: 277281.
   Google Scholar
• Gorbalenya, A. E., Koonin, E. V., Donchenko, A. P. and Blinov, V. M. (1988a). A conserved NTP- motif in putative helicases. Nature 333: 22.
   PubMed Web of Science ®Google Scholar
• Gorbalenya, A. E., Koonin, E. V., Donchenko, A. P., and Blinov, V. M. (1988b). A novel superfam- ily of nucleoside triphosphate-binding motif containing proteins which are probably involved in duplex unwinding in DNA and RNA replication and recombination. FEBS Lett. 235: 16—24.
   PubMed Web of Science ®Google Scholar
• Gorbalenya, A. E., Koonin, E. V., Donchenko, A. P., and Blinov, V. M. (1989). Two related super- families of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes. Nucleic Acids Res. 17: 4713—4730.
   PubMed Web of Science ®Google Scholar
• Grifo, J. A., Tahara, S. M., Abramson, R. D., Satler, C. A., and Merrick, W. C. (1984). RNA-stimu- lated ATPase activity of eukaryotic initiation factors. J. Biol. Chem. 259: 8648—8654.
   PubMed Web of Science ®Google Scholar
• Grivell, L. A. (1995). Nucleo-mitochondrial interactions in mitochondrial gene expression. Crit. Rev. Biochem. Mol. Biol. 30: 121—164.
   PubMed Web of Science ®Google Scholar
• Gros, C. and Wengler, G. (1996). Identification of an RNA-stimulated NTPase in the predicted he- licase sequence of the Rubella virus nonstruc- tural polyprotein. Virology 217: 367—372.
   Google Scholar
• Gururajan, R., Mathews, L., Longo, F. J. and Weeks, D. L. (1994). An3 mRNA encodes an RNA helicase that colocalizes with nucleoli in Xe- nopus oocytes in a stage-specific manner. Proc. Natl. Acad. Sci. USA 91: 2056—2060.
   PubMedGoogle Scholar
• Gururajan, R., Perry O'Keefe, H., Melton, D. A., and Weeks, D. L. (1991). The Xenopus localized messenger RNA An3 may encode an ATP- dependent RNA helicase. Nature 349: 717719.
   Google Scholar
• Gururajan, R. and Weeks, D. L. (1997). An3 protein encoded by a localized maternal mRNA in Xenopus laevis is an ATPase with substrate- specific RNA helicase activity. Biochim. Bio- phys. Acta 1350: 169—182.
   PubMedGoogle Scholar
• Hagan, K. W., Ruiz-Echevarrfa, M. J., Quan, Y., and Peltz, S. W. (1995). Characterization of cis-acting sequences and decay intermediates involved in nonsense-mediated mRNA turnover. Mol. Cell. Biol. 15: 809—823.
   PubMedGoogle Scholar
• Hajduk, S. L., Harris, M. E., and Pollard, V. W. (1993). RNA editing in kinetoplastid mitochondria. FASEB J. 7: 54—63.
   PubMedGoogle Scholar
• Hamm, J. and Lammond, A. I. (1998). Spliceosome assembly: the unwinding role of DEAD-box proteins. Curr. Biol. 8: 532—534.
   PubMedGoogle Scholar
• Hay, B., Jan, L. Y., and Jan, Y. N. (1988). A protein component of Drosophila polar granules is encoded by vasa and has extensive sequence similarity to ATP-dependent helicases. Cell 55: 577—587.
   PubMed Web of Science ®Google Scholar
• He, F. and Jacobson, A. (1995). Identification of a novel component of the nonsense-mediated mRNA decay pathway using an interacting protein screen. Genes Dev. 9: 437—454.
   PubMedGoogle Scholar
• Hershey, J. W. B. (1991). Translational control in mammalian cells. Annu. Rev. Biochem. 60: 117755.
   Google Scholar
• Hirling, H., Scheffner, M., Restle, T., and Stahl, H. (1989). RNA helicase activity associated with the human p68 protein. Nature 339: 562—564.
   PubMed Web of Science ®Google Scholar
• Hodgeman, T. C. (1988). A new superfamily of replicative proteins. Nature 333: 22—23.
   Google Scholar
• Houghton, M., Selby, M., Weiner, A., and Choo, Q. L. (1994). Hepatits C virus: structure, protein products and processing of the polyprotein precursor. Curr. Stud. Hematol. Blood Trans- fus. 61: 1—11.
   Google Scholar
• Humphries, R. K., Ley, T. J., Anagnou, N. P., Baur, A. W., and Nienhuis, A. W. (1984). b0- Thalassemia gene: A premature termination codon causes b-mRNA deficiency without affecting cytoplasmic b-mRNA stability. Blood 64: 23—32.
   PubMed Web of Science ®Google Scholar
• Iggo, R. D., Jamieson, D.J., MacNeill, S. A., Southgate, J., McPheat, J., and Lane, D. P. (1991). p68 RNA helicase: identification of a nucleolar form and cloning of related genes containing a conserved intron in yeasts. Mol. Cell. Biol. 11: 1326—1333.
   PubMedGoogle Scholar
• Iggo, R. D. and Lane, D. P. (1989). Nuclear protein p68 is an RNA-dependent ATPase. EMBO J. 8: 1827—1831.
   PubMed Web of Science ®Google Scholar
• Jamieson, D. J. and Beggs, J. D. (1991). A suppressor of yeast spp81/ded1 mutations encodes a very similar putative ATP-dependent RNA he- licase. Mol. Microbiol. 5: 805—812.
   PubMedGoogle Scholar
• Jamieson, D. J., Rahe, B., Pringle, J., and Beggs, J. D. (1991). A suppressor of a yeast splicing mutation (prp8—1) encodes a putative ATP- dependent RNA helicase. Nature 349: 715717.
   Google Scholar
• Jaramillo, M., Dever, T. E., Merrick, W. C., and Sonenberg, N. (1991). RNA unwinding in translation: assembly of helicase complex intermediates comprising eukaryotic initiation factors eIF-2F and eIF-4B. Mol. Cell. Biol. 11: 59925997.
   Google Scholar
• Jin, L. and Peterson, D. L. (1995). Expression, isolation, and characterization of the Hepatitis C virus ATPase/RNA helicase. Arch. Biochem. Biophys. 323: 47—53.
   Google Scholar
• Jones, P. G., Mitta, M., Kim, Y., Jiang, W., and Inouye, M. (1996). Cold shock induces a major ribosomal-associated protein that unwinds double-stranded RNA in Escherichia coli. Proc. Natl. Acad. Sci. USA 93: 76—80.
   PubMed Web of Science ®Google Scholar
• Kadare, G. and Haenni, A. L. (1997). Virus encoded RNA helicases, J. Virol. 71: 2583—2590.
   PubMed Web of Science ®Google Scholar
• Kalman, M., Murphy, H., and Cashel, M. (1991). rhlB, a new Escherichia coli K-12 gene with an RNA helicase-like protein sequence motif, one of the least five such possible genes in a prokary- ote. New Biol. 3: 886—895.
   PubMedGoogle Scholar
• Kim, D. W., Gwack, Y., Han, J. H., and Choe, J. (1995). C-terminal domain of the hepatitis C virus protein contains an RNA helicase activity. Biochem. Biophys. Res. Commun. 215: 160166.
   Google Scholar
• Kim, J., Ljungdahl, P. O., and Fink, G. R. (1990). kem mutations affect nuclear fusion in Saccharomyces cerevisiae. <i>Genetics126: 799812.
   Google Scholar
• Kim, S. H., Smith, J., Claude, A., and Lin, R. J. (1992). The purified yeast pre-mRNA splicing factor PRP2 is an RNA-dependent NTPase. EMBO J. 11: 2319—2326.
   PubMedGoogle Scholar
• King, P. S. and Beggs, J. D. (1990). Interaction of the PRP2 protein with pre-mRNA splicing complexes in Saccharomyces cerevisiae. Nucleic Acids Res. 18: 6559—6564.
   PubMedGoogle Scholar
• Kipling, D., Tambini, C., and Kearsey, S. E. (1991). rar mutations which increase artificial chromosome stability in Saccharomyces cerevisiae identify transcription and recombination proteins. Nucleic Acids Res. 19: 1385—1391.
   PubMedGoogle Scholar
• Klug, A. and Schwabe, J. W. (1995). Protein motifs 5. Zinc fingers. FASEB J. 9: 597—604.
   PubMed Web of Science ®Google Scholar
• Komiya, T., Itoh, K., Ikenishi, K., and Furusawa, M. (1994). Isolation and characterization of a novel gene of the DEAD box protein family which is specifically expressed in germ cells of Xenopus laevis. Dev. Biol. 162: 354363.
   Google Scholar
• Komiya, T. and Tanigawa, Y. (1995). Cloning of a gene of the DEAD box protein family which is specifically expressed in germ cells in rats. Bio- chem. Biophys. Res. Commun. 207: 405410.
   Google Scholar
• Koonin, E. V. (1991). Similarities in RNA heli- cases. Nature 352: 290.
   PubMed Web of Science ®Google Scholar
• Koonin, E. V. (1992). A new group of putative RNA helicases. Trends Biochem. Sci. 17: 495497.
   Google Scholar
• Koonin, E. V. and Senkevich, T. G. (1992). Vaccinia virus encodes four putative DNA and/or RNA helicases distantly related to each other. J. Gen.Virol. 73: 989—993.
   Google Scholar
• Kozak, M. (1989). The scanning model for translation: An update. J. Cell. Biol. 108: 229—241.
   PubMed Web of Science ®Google Scholar
• Kramer, A. (1996). The structure and function of proteins involved in mammalian pre-mRNA splicing. Annu. Rev. Biochem. 65: 367—409.
   PubMed Web of Science ®Google Scholar
• Kressler, D., de la Cruz, J., Rojo, M., and Linder, P. (1997). Fal1p is an essential DEAD-box protein involved in 40S-ribosomal-subunit biogenesis in Saccharomyces cerevisiae. Mol. Cell. Biol. 17: 7283—7294.
   Google Scholar
• Kressler, D., de la Cruz, J., Rojo, M., and Linder, P. (1998). Dbp6p is an essential putative ATP- dependent RNA helicase required for the 60S- ribosomal-subunit assembly in Saccharomyces cerevisiae. Mol. Cell. Biol. 18: 1855—1865.
   PubMed Web of Science ®Google Scholar
• Kuroda, M. I., Kernan, M. J., Kreber, R., Ganetzky, B., and Baker, B. S. (1991). The maleless protein associates with the X chromosme to regulate dosage compensation in Drosophila. <i>Cell66: 935—947.
   Google Scholar
• Laggerbauer, B., Achsel, T., and Luhrmann, R. (1998). The human U5—200kD DEXH-box protein unwinds U4/U6 duplices in vitro. Proc. Natl. Acad. Sci. USA 95: 4188—4192.
   PubMed Web of Science ®Google Scholar
• Lain, S., Riechmann, J. L., and Garcia, J. A. (1990). RNA helicase: a novel activity associated with a protein encoded by a postive strand RNA virus. Nucleic Acids Res. 18: 7003—7006.
   PubMed Web of Science ®Google Scholar
• Lambowitz, A. M. and Belfort, M. (1993). Introns as mobile genetic elements. Annu. Rev. Biochem. 62: 587—622.
   PubMed Web of Science ®Google Scholar
• Lambowitz, A. M., Caprara, M. G., Zimmerly, S., and Perlman, P. S. (1998). Group I and group II ribozymes as RNPs: Clues to the past and guides to the future. In: T. Cech (ed.) The RNA World, 2nd edition, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, in press.
   Google Scholar
• Lambowitz, A. M. and Perlman, P. S. (1990). Involvement of aminoacyl-tRNA synthetases and other proteins in group I and group II intron splicing. Trends Biochem. Sci. 15: 440—444.
   PubMed Web of Science ®Google Scholar
• Lamm, G. M. and Lamond, A. I. (1993). Non- snRNP protein splicing factors. Biochim. Biophys. Acta 1173: 247—265.
   PubMedGoogle Scholar
• Lamond, A. I. (1993). The spliceosome. Bio Essays 15: 595—603.
   PubMedGoogle Scholar
• Lane, D. P. and Hoeffler, W. K. (1980). SV40 large T shares an antigenic determinant with a cellular protein of molecular weight 68,000. Nature 288: 167—170.
   PubMed Web of Science ®Google Scholar
• Larimer, F. W., Hsu, C. L., Maupin, M. K., and Stevens, A. (1992). Characterization of the XRN1 gene encoding a 5'®3'exoribonuclease: sequence data and analysis of disparate protein and mRNA levels of the gene-disrupted yeast cells. Gene 120: 51—57.
   PubMedGoogle Scholar
• Lasko, P. F. and Ashburner, M. (1988). The product of the Drosophila gene vasa is very similar to eukaryotic initiation factor 4A. Nature 335: 611—617.
   PubMed Web of Science ®Google Scholar
• Lasko, P. F. and Ashburner, M. (1990). Posterior localization of vasa protein correlates with, but is not sufficient for, pole cell development. Genes Dev. 4: 905—922.
   PubMedGoogle Scholar
• Laughrea, M. and Moore, P. B. (1978). On the relationship between the binding of ribosomal protein S1 to the 30S subunit of Escherichia coli and the 3' terminus of 16S RNA. J. Mol. Biol. 121: 411—430.
   Google Scholar
• Lee, C.-G., Chang, K., A., Kuroda, M. I., and Hurwitz, J. (1997). The NTPase/helicase activities of Drosophila maleless, an essential factor in dosage compensation. EMBO J. 16: 2671681.
   Google Scholar
• Lee, C.-G. and Hurwitz, J. (1992). A new RNA helicase isolated from Hela cells that catalyti- cally translocated in the 3' to 5' direction. J. Biol. Chem. 267: 4398—4407.
   PubMedGoogle Scholar
• Lee, C.-G. and Hurwitz, J. (1993). Human RNA helicase A is homologous to the maleless protein of Drosophila. J. Biol. Chem. 268: 1682216830.
   Google Scholar
• Leeds, P., Peltz, S. W., Jacobson, A., and Culbertson, M. R. (1991). The product of the yeast UPF1 gene is required for rapid turnover of mRNAs containing a premature translational termination codon. Genes Dev. 5: 2303—2314.
   PubMed Web of Science ®Google Scholar
• Leroy, P., Alzari, P., Sassoon, D., Wolgemuth, D., and Fellous, M. (1989). The protein encoded by a murine male germ cell-specific transcript is a putative ATP-dependent RNA helicase. Cell 57: 549—559.
   PubMedGoogle Scholar
• Liang, L., Diehl-Jones, W., and Lasko, P. (1994). Localization of vasa protein to the Drosophila pole plasm is independent of its RNA-bindig and helicase activities. Development 120: 12011211.
   Google Scholar
• Liang, S., Hitomi, M., Hu, Y. H., Liu, Y., and Tartakoff, A. M. (1996). A DEAD-box-family protein is required for nucleocytoplasmic transport of yeast mRNA. Mol. Cell. Biol. 16: 51395146.
   Google Scholar
• Lin, R.-J., Lustig, A. J., and Abelson, J. N. (1987). Splicing of yeast nuclear pre-mRNA in vitro requires a functional 40S spliceosome and several extrinsic factors. Genes Dev. 1: 7—18.
   PubMedGoogle Scholar
• Linder, P., Lasko, P. F., Ashburner, M., Leroy, P., Nielsen, P. P., Nishi, K., Schnier, J., and Slonimski, P. P. (1989). Birth of the D-E-A-D box. Nature 337: 121—122.
   PubMed Web of Science ®Google Scholar
• Linder, P. and Prat, A. (1990). Baker's yeast, the new work horse in protein synthesis studies: Analyzing eukaryotic translation initiation. Bio Essays 12: 519—527.
   PubMedGoogle Scholar
• Linder, P. and Slonimski, P. P. (1988). Sequence of the genes TIF1 and TIF2 from Saccharo- myces cerevisiae coding for a translation initiation factor. Nucleic Acids Res. 16: 10359.
   PubMed Web of Science ®Google Scholar
• Linder, P. and Slonimski, P. P. (1989). An essential yeast protein, encoded by the duplicated genes Tif 1 and Tif2 and homologous to the mammalian translation initiation factor eIF- 4A, can suppress a mitochondrial missense mutation. Proc. Natl. Acad. Sci. USA 86: 22862290.
   Google Scholar
• Lu, K. P. and Means, A. R. (1993). Regulation of the cell cycle by calcium and calmodulin. Endo- crin. Rev. 14: 40—58.
   PubMed Web of Science ®Google Scholar
• Lucchesi, J. C. and Manning, J. E. (1987). Gene dosage compensation in Drosophila melano- gaster. Adv. Genet. 24: 371—429.
   PubMedGoogle Scholar
• Madhani, H. D. and Guthrie, C. (1994a). Dynamic RNA-RNA interactions in the spliceosome. Annu. Rev. Genet. 28: 1—26.
   PubMedGoogle Scholar
• Madhani, H. D. and Guthrie, C. (1994b). Genetic interaction between the yeast RNA helicase homolog Prp16 and spliceosomal snRNAs identify candidate ligands for the Prp16 RNA- dependent ATPase. Genetics 137: 677—687.
   PubMed Web of Science ®Google Scholar
• Maekawa, H., Nakagawa, T., Uno, Y., Kitamura, K., and Shimoda, C. (1994). The ste13+ gene encoding a putative RNA helicase is essential for nitrogen starvation-induced G1 arrest and initiation of sexual development in the fission yeast Schizosaccharomyces pombe. Mol. <i>Gen. Genet. 244: 456—464.
   Google Scholar
• Mahowald, A. P. (1971). Polar granules of Droso- phila. III. The continuity of polar granules during the life-cycle of Drosohpila. J. <i>Exp. Zool. 176: 329—344.
   Google Scholar
• Mahowald, A. P. (1992). Germ plasm revisited and illuminated. Science 255: 1216—1217.
   PubMed Web of Science ®Google Scholar
• Margossian, S.P. and Butow, R. A. (1996). RNA trunover and the control of mitochondrial gene expression. Trends Biochem. Sci. 21: 392396.
   Google Scholar
• Margossian, S. P., Li, H., Zassenhaus, H. P., and Butow, R. A. (1996). The DExH box protein Suv3p is a component of a yeast mitochon- drial 3'- to- 'Exoribonuclease that suppresses group I intron toxicty. Cell 84: 199—209.
   PubMed Web of Science ®Google Scholar
• Matson, S. W. and Kaiser-Rogers, K. A. (1990). DNA helicases. Annu. Rev. Biochem. 59: 289329.
   Google Scholar
• Mehlin, H., Daneholt, B., and Skoglund, U. (1992). Translocation of a specific premessenger ribo- nucleoprotein particle through the nuclear pore studied with electron microscope tomography. Cell 69: 605—613.
   PubMed Web of Science ®Google Scholar
• Michel, F., Umesono, K., and Ozeki, H. (1989). Comparative and functional anatomy of group II catalytic introns: a review. Gene 82: 5—30.
   PubMed Web of Science ®Google Scholar
• Milburn, S. C., Hershey, J. W. B., Davies, M. V., Kellcher, K., and Kaufman, R. J. (1990). Cloning and sequencing of eukaryotic initiation factor 4B cDNA: sequence determination identifies a common RNA recognition motif. EMBO J. 9: 2783—2790.
   PubMed Web of Science ®Google Scholar
• Missel, A. and Goringer, H. U. (1994). Trypanosoma brucei mitochondria contain RNA helicase activity. Nucleic Acids Res. 22: 4050—4056.
   PubMedGoogle Scholar
• Missel, A., Souza, A. E., Norskau, G. and Goringer, H. U. (1997). Disruption of a gene encoding a novel mitochondrial DEAD-box protein in Try- panosoma brucei affects edited mRNAs. Mol. Cell. Biol. 17: 4895—4903.
   PubMedGoogle Scholar
• Moazed, D. and Noller, H. F. (1991). Sites of the CCA end of peptidyl-tRNA with 23S rRNA. Proc. Natl. Acad. Sci. USA 88: 3725—3728.
   PubMed Web of Science ®Google Scholar
• Moore, M. J., Query, C. C., and Sharp, P. A. (1993). Splicing of precursors to messenger RNAs by the spliceosome. In: R. F. Gesteland and J. F. Atkins (eds.) The RNA World. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, pp. 303—357.
   Google Scholar
• Nicol, S. M. and Fuller-Pace, F. V. (1995). The “DEAD box” protein DbpA interacts specifically with the peptidyltransferase center in 23S rRNA. Proc. Natl. Acad. Sci. USA 92: 1168111685.
   Google Scholar
• Nielsen, P. J. and Trachsel, H. (1988). The mouse protein synthesis initiation factor 4A gene family includes two related functional genes which are differentially expressed. EMBO J. 7: 20972105.
   Google Scholar
• Niemer, I., Schmelzer, C., and Borner, G. V. (1995). Overexpression of DEAD box protein pMSS116 promotes ATP-dependent splicing of a yeast group II intron in vitro. Nucleic Acids Res. 23: 2966—2972.
   Google Scholar
• Nierhaus, K. H. (1991). The side-by-side model of two tRNA molecules allowing the alpha-helical conformation of the nascent polypeptide during the ribosomal transpeptidation. Biochimie 73: 947—60.
   Google Scholar
• Nishi, K., Morel-Deville, F., Hershey, J. W. B., Leighton, T., and Schnier, J. (1988). An eIF- 4A-like protein is a suppressor of an Escheri- chia coli mutant defective in 50S ribosome sub- unit assembly. Nature 336: 496—498.
   PubMed Web of Science ®Google Scholar
• Noller, H. F. (1991). Ribosomal RNA and translation. Annu. Rev. Biochem. 60: 191—227.
   PubMed Web of Science ®Google Scholar
• O'Day, C. L., Chavanikamannil, F., and Abelson, J. N. (1996a). 18S rRNA processing requires the RNA helicase-like protein Rpr3. Nucleic Acids Res. 24: 3201—3207.
   Google Scholar
• O'Day, C. L., Dalbadie-McFarland, G., and Abelson, J. N. (1996b). The Saccharomyces cerevisiae Prp5 protein has RNA-dependent ATPase activity with specificity for U2 small nuclear RNA. J. Biol. Chem. 271: 3326133267.
   Google Scholar
• Ohno, M. and Shimura, Y. (1996). A human RNA helicase-like protein, HRH1, facilitates nuclear export of spliced mRNA by releasing RNA from spliceosome. Genes Dev. 10: 997—1007.
   PubMedGoogle Scholar
• Ono, Y., Ohno, M., and Shimura, Y. (1994). Identification of a putative RNA helicase (HRHI), a human homolog of yeast Prp22. Mol. Cell. Biol. 14: 6711—7620.
   Google Scholar
• Owttrim, G. W., Hof Mann, S., and Kuhlemeier, C. (1991). Divergent genes for translation initiation factor eIF-4A are coordinately expressed in tobacco. Nucleic Acids Res. 19: 5491—5496.
   PubMed Web of Science ®Google Scholar
• Pacha, R. F., Meis, R., and Condit, R. C. (1990). Structure and expression of the vaccinia virus gene which prevents virus-induced breakdown of RNA. J. Virol. 64: 3853—3863.
   Google Scholar
• Paoletti, E., Rosemond-Hornbeak, H., and Moss, B. (1974). Two nucleic acid-dependent nucleo- side triphosphate phosphohydrolases from vaccinia virus. Purification and characterization. J. Biol. Chem. 249: 3273—3280.
   PubMed Web of Science ®Google Scholar
• Patterson, L. F., Harvey, M., and Lasko, P. F. (1992). Dbp73D, a Drosophila gene expressed in ovary, encodes a novel DEAD box protein. Nucleic Acids Res. 20: 3063—3067.
   Google Scholar
• Pause, A., Methot, N., and Sonenberg, N. (1993). The HRIGRXXR region of the DEAD box RNA helicase eukaryotic translation factor 4A is required for RNA binding and ATP hydrolysis. Mol. Cell. Biol. 13: 6789—6798.
   PubMed Web of Science ®Google Scholar
• Pause, A. and Sonenberg, N. (1992). Mutational analysis of a DEAD box RNA helicase: the mammalian translation initiation factor eIF-4A. EMBO J. 11: 2643—2654.
   PubMedGoogle Scholar
• Peltz, S. W., Feng, H., Welch, E., and Jacobson, A. (1994). Nonsense-mediated mRNA decay in yeast. Prog. Nucleic Acids Res. Mol. Biol. 47: 271—298.
   PubMedGoogle Scholar
• Plumpton, M., McGarvey, M., and Beggs, J. D. (1994). A dominant negative mutation in the conserved RNA helicase motif 'SAT' causes splicing factor PRP2 to stall in spliceosomes. EMBO J. 13: 879—887.
   PubMed Web of Science ®Google Scholar
• Prat, A., Schmid, S. R., Buser, P., Blum, S., Trachsel, H., Nielsen, P. J., and Linder, P. (1990). Expression of translation initiation factor eIF-4A from yeast and mouse in Saccharomyces cere- visiae. Biochim. Biophys. Acta 1050: 140—145.
   PubMedGoogle Scholar
• Py, B., Higgins, C. F., Krisch, H. M., and Carpousis, A. J. (1996). A DEAD-box RNA helicase in the Escherichia coli degradosome. Nature 381: 169—172.
   PubMed Web of Science ®Google Scholar
• Raghunathan, P. L. and Guthrie, C. (1998). RNA unwinding in U4-U6 snRNPs requires ATP hydrolysis and the DEIH-box splicing factor Brr2. Curr. Biol. 8: 847—855.
   PubMed Web of Science ®Google Scholar
• Ray, B. K., Lawson, T. G., Kramer, J. C., Cladaras, M. H., Grifo, J. A., Abramson, R. D., Merick, W. C., and Thach, R. E. (1985). ATP-depen- dent unwinding of messenger RNA structure by eukaryotic initiation factors. J. Biol. Chem. 260: 7651—7658.
   PubMed Web of Science ®Google Scholar
• Rhoads, R. E. (1991) Initiation: mRNA and 60S subunit binding. In: H. Trachsel (ed.) Translation in Eukaryotes, CRC Press, Boca Raton, Florida, pp. 109—148.
   Google Scholar
• Ripmaster, T. L., Vaughn, G. P., and Woolford, J. L. Jr. (1992). A putative ATP-dependent RNA helicase involved in Saccharomyces cerevi- siae ribosome assembly. Proc. Natl. Acad. Sci. USA 89: 11131—11135.
   PubMedGoogle Scholar
• Roussell, D. L. and Bennett, K. L. (1993). glh-1, a germ-line putative RNA helicase from Caenor- habditis, has four zinc fingers. Proc. Natl. Acad. Sci. USA 90: 9300—9304.
   PubMed Web of Science ®Google Scholar
• Roy, J., Kyunghoon, K., Maddock, J., Anthony, J. G. and Woolford, J. L. Jr. (1995). The final stages of spliceosome maturation require Spp2p that can interact with the DEAH box protein Prp2p and promte step 1 of splicing. RNA 1: 375—390.
   PubMed Web of Science ®Google Scholar
• Rozen, F., Edery, I., Meeovitch, K., Dever, T. E., Merrick, W. C., and Sonenberg, N. (1990). Bidirectional RNA helicase activity of eukary- otic translation initiation factors 4A and 4F. Mol. Cell. Biol. 10: 1134—1144.
   PubMed Web of Science ®Google Scholar
• Rozen, F., Pelltier, J., Trachsel, H., and Sonenberg, N. (1989). A lysine substitution in the ATP binding site of eukaryotic initiation factor 4A abrogates nucleotide-binding activity. Mol. Cell. Biol. 9: 4061—4063.
   PubMedGoogle Scholar
• Ruby, S. W. and Abelson, J. (1991). Pre-mRNA splicing in yeast. Trends Genet. 7: 79—85.
   PubMedGoogle Scholar
• Sachs, A. B. and Davis, R. W. (1990). Translation initiation and ribosomal biogenesis: Involvement of a putaive rRNA helicase and RPL46. Science 247: 1077—1079.
   PubMed Web of Science ®Google Scholar
• Schmid, S. R. and Linder, P. (1991). Translation initiation factor 4A from Saccharomyces cer- evisiae: analysis of residues conserved in the D-E-A-D family of RNA helicases. Mol. Cell. Biol. 11: 3463—3471.
   PubMedGoogle Scholar
• Schmid, S. R. and Linder, P. (1992). D-E-A-D protein family of putative RNA helicases. Mol. Microbiol. 6: 283—291.
   PubMed Web of Science ®Google Scholar
• Schwer, B. and Guthrie, C. (1991). PRP16 is an RNA-dependent ATPase that interacts transiently with the spliceosome. Nature 349: 494499.
   Google Scholar
• Seedorf, M. and Silver, P. A. (1997). Importin/ karyopherin protein family members required for mRNA export from the nucleus. Proc. Natl. Acad. Sci. USA 94: 8590—8595.
   PubMedGoogle Scholar
• Seraphin, B., Boulet, A., Simon, M., and Faye, G. (1987). Construction of a yeast strain devoid of mitochondrial introns and its use to screen nuclear genes involved in mitochondrial splicing. Proc. Natl. Acad. Sci. USA 84: 6810—6814.
   PubMed Web of Science ®Google Scholar
• Seraphin, B., Simon, M., Boulet, A., and Faye, G. (1989). Mitochondrial splicing requires a protein from a novel helicase family. Nature 337: 84—87.
   PubMed Web of Science ®Google Scholar
• Shuman, S. (1992). Vaccina virus RNA helicase: An essential enzyme related to the DE-H family of RNA-dependent NTPases. Proc. Natl. Acad. Sci. USA 89: 10935—10939.
   PubMed Web of Science ®Google Scholar
• Shuman, S. (1993). Vaccina virus RNA helicase. Directionality and substrate specifity. J. Biol. Chem. 268: 11798—11802.
   PubMedGoogle Scholar
• Snay-Hodge, C. A., Colot, H. V., Goldstein, A. L., and Cole, C. N. (1998). Dbp5p/rat8p is a yeast nuclear pore-associated DEAD-box protein essential for RNA export. EMBO J. 17: 26632676.
   Google Scholar
• Sollner-Webb, B. (1996). Trypanosome RNA editing: resolved. Science 273: 1182—1183.
   PubMedGoogle Scholar
• Sonenberg, N. (1988). Cap-binding proteins of eukaryotic messenger RNA: functions in initiation and control of translation. Prog. Nucleic Acids Res. Mol. Biol. 35: 173—207.
   PubMed Web of Science ®Google Scholar
• Song, Y., Kim, S., and Kim, J. (1995). ROK1, a high-copy-number plasmid suppressor of kem1, encodes a putative ATP-dependent RNA he- licase in Saccharomyces cerevisiae. <i>Gene166: 151—154.
   Google Scholar
• Stade, K., Ford, C. S., Guthrie, C., and Weis, K. (1997). Exportin 1 (Crm1p) is an essential nuclear export factor. Cell 90: 1041—1050.
   PubMed Web of Science ®Google Scholar
• Staley, J. P. and Guthrie, C. (1998). Mechanical devices of the spliceosome: motors, clocks, springs, and things. Cell 92: 315—326.
   PubMed Web of Science ®Google Scholar
• Stepien, P. P., Kokot, L., Leski, T., and Bartnik, E. (1995). The suv3 nuclear gene product is required for the in vivo processing of the yeast mitochondrial 21S rRNA transcripts containing the r1 intron. Curr. Genet. 27: 234—238.
   Google Scholar
• Stepien, P. P., Margossian, S. P., Landsman, D., and Butow, R.A. (1992). The nuclear gene suv3 affecting mitochondrial post-transcriptional processes encodes a putative ATP-dependent RNA helicase. Proc. Natl. Acad. Sci. USA 89: 6813—6817.
   PubMed Web of Science ®Google Scholar
• Strauss, E. and Guthrie, C. (1991). A cold-sensitive mRNA splicing mutant is a member of the RNA helicase gene family. Genes Dev. 5: 629641.
   Google Scholar
• Strauss, E. and Guthrie, C. (1994). PRP28, a 'DEAD-box' protein, is required for the first step of mRNA splicing in vitro. Nucleic Acids Res. 22: 3187—3193.
   PubMedGoogle Scholar
• Strome, S. (1992). The germ of the issue. Nature 358: 368—369.
   Google Scholar
• Sudo, K., Takahashi, E., and Nakamura, Y. (1995). Isolation and mapping of the human EIF4A2 gene homologous to the murine protein synthesis initiation factor 4A-II gene Eif4a2. Cyto- genet. Cell Genet:. 71: 385—388.
   PubMedGoogle Scholar
• Szer, W., Hermoso, J. M., and Boublik, M. (1976). Destabilization of the secondary structure of RNA by ribosomal protein S1 from Escherichia coli. Biochem. Biophys. Res. Comm. 70: 957—964.
   Google Scholar
• Takeshita, K., Forget, B. G., Scaarpa, A., and Benz, E. J. (1984). Intranuclear defect in b-globin mRNA accumulation due to a premature translation termination codon. Blood 64: 13—22.
   PubMed Web of Science ®Google Scholar
• Tang, H., Gaietta, G. M., Fischer, W. H., Ellisman, M. H., and Wong, S. F. (1997). A cellular cofactor for the constitutive transport element of type D retrovirus. Science 276: 1412—1415.
   PubMed Web of Science ®Google Scholar
• Teigelkamp, S., McGarvey, M., Plumpton, M., and Beggs, J. D. (1994). The splicing factor PRP2, a putative RNA helicase, interacts directly with the pre-mRNA. EMBO J. 13: 888—897.
   PubMedGoogle Scholar
• Tishkoff, D. X., Johnson, A. W., and Kolodner, R. D. (1991). Molecular and genetic analysis of the gene encoding the Saccharomyces cerevisiae strand exchange protein Sep1. Mol. Cell. Biol. 11: 2593—2608.
   PubMedGoogle Scholar
• Toone, W. M., Rudd, K. E., and Friesen, J. D. (1991). deaD, a new Escherichia coli gene encoding a presumed ATP-dependent RNA helicase, can suppress a mutation in rpsB gene encoding ri- bosomal Protein S2. J. Bacteriol. 173: 32913302.
   Google Scholar
• Tseng, S., Weaver, P. L., Liu, Y., Hitomi, M., Tartakoff, A. M., and Chang, T.-H. (1998). Dbp5p, a cytosolic RNA helicase, is required for poly(A)+ RNA export. EMBO J. 17: 26512662.
   Google Scholar
• Ullman, K. S., Powers, M. A., and Forbes, D. J. (1997). Nuclear export receptors: from impor- tin to exportin. Cell 90: 967—970.
   PubMedGoogle Scholar
• Umen, J. G. and Guthrie, C. (1995a). Prp16p, Slu7p, and Prp8p interact with the 3'splice site in two distinct stages during the second catalytic step of pre-mRNA splicing. RNA 1: 584—597.
   PubMedGoogle Scholar
• Umen, J. G. and Guthrie, C. (1995b). The second catalytic step of pre-mRNA splicing. RNA 1: 869—885.
   PubMed Web of Science ®Google Scholar
• Venema, J., Bousquet-Antonelli, C., Gelugne, J.-P., Caizergues-Ferrer, M., and Tollervey, D. (1997). Rok1 is a putative RNA helicase required for rRNA processing. Mol. Cell. Biol. 17: 33983407.
   Google Scholar
• Voorma, H. O., Thomas, A. A. M., and van Heugten, H. A. A. (1994). Initiation of protein synthesis in eukaryotes. Mol. Biol. Rep. 19: 139—145.
   Google Scholar
• Wagner, J. D. O., Jankowsky, E., Company, M., Pyle, A. M., and Abelson, J. N. (1998). The DEAH-box protein PRP22 is an ATPase that mediates ATP-dependent mRNA release from the spliceosome and unwinds RNA. EMBO J. 17: 2926—2937.
   PubMed Web of Science ®Google Scholar
• Walker, J. E., Saraste, M., Runswick, M. J., and Gay, N. J. (1982). Distantly related sequence in the a- and b-subunits of ATP synthase, myo- sin, kinase and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1: 945—951.
   PubMed Web of Science ®Google Scholar
• Wang, Y., Wagner, J. D. O., and Guthrie, C. (1998). The DEAH-box splicing factor Prp16 unwinds RNA duplexes in vitro. Curr. Biol. 8: 441451.
   Google Scholar
• Warrener, P. and Collett, M. S. (1995). Pestivirus NS3 (p80) protein possesses RNA helicase activity. J. Virol. 69: 1720—1726.
   Google Scholar
• Wassarman, D. A. and Steitz, J. A. (1991). Alive with DEAD proteins. Nature 349: 463—464.
   PubMedGoogle Scholar
• Weaver, P. L., Sun, C., and Chang, T.-H. (1997). Dbp3p, a putative RNA helicase in Saccharo- myces cerevisiae, is required for efficient pre- rRNA processing predominantly at site A3. Mol. Cell. Biol. 17: 1354—1365.
   PubMed Web of Science ®Google Scholar
• Will, C. L., and Luhrmann, R. (1997). Protein functions in pre-mRNA splicing. Curr. Opin. Cell. Biol. 9: 320—328.
   PubMed Web of Science ®Google Scholar
• Yanez, R. J., M., R. J., Boursnell, M., Rodriguez, J. F., and Vinuela, E. (1993). Two putative African swine fever virus helicases similar to yeast 'DEAH' pre-mRNA processing proteins and vaccinia virus ATPases D11L and D6R. Gene 134: 161—174.
   Google Scholar
• Zassenhaus, H. P., Farrelly, F., Hudspeth, M. E., Grossman, L. I., and Butow, R. A. (1983). Transcriptional analysis of the Saccharomyces cer- evisiae mitochondrial var1 gene: anomalous hybridization of RNA from AT-rich regions. Mol. Cell. Biol. 3: 1615—1624.
   PubMedGoogle Scholar
• Zhu, H., Conrad-Webb, H., Liao, X. S., Perlman, P.S., and Butow, R. A. (1989). Functional expression of a yeast mitochondrial intron-encod- ed protein requires RNA processing at a conserved dodecamer sequence at the 3'end of the gene. Mol. Cell. Biol. 9: 1507—1512.
   PubMedGoogle Scholar