DRS1 to DRS7, Novel Genes Required for Ribosome Assembly and Function in Saccharomyces cerevisiae

References

• Andrew, C., A. K. Hopper, and B. D. Hall. 1976. A yeast mutant defective in the processing of 27S rRNA precursor. Mol. Gen. Genet. 144:29–37.
   PubMedGoogle Scholar
• Baim, S. B., D. F. Pietras, D. C. Eustice, and F. Sherman. 1985. A mutation allowing an mRNA secondary structure diminishes translation of Saccharomyces cerevisiae iso-1-cytochrome c. Mol. Cell. Biol. 5:1839–1846.
   PubMedGoogle Scholar
• Bayliss, F. T., and J. L. Ingraham. 1974. Mutation in Saccharomyces cerevisiae conferring streptomycin and cold sensitivity by affecting ribosome formation and function. J. Bacteriol. 118:319–328.
   PubMed Web of Science ®Google Scholar
• Beltrán, C., J. Kopecky, Y.-C. E. Pan, H. Nelson, and N. Nelson. 1992. Cloning and mutational analysis of the gene encoding subunit C of yeast vacuolar H+-ATPase. J. Biol. Chem. 267: 774–779.
   PubMed Web of Science ®Google Scholar
• Bender, A., and J. R. Pringle. 1991. Use of a screen for synthetic lethal and multicopy suppressee mutants to identify two new genes involved in morphogenesis in Saccharomyces cerevisiae. Mol. Cell. Biol. 11:1295–1305.
   PubMed Web of Science ®Google Scholar
• Cantor, C. R., and P. R. Schimmel. 1980. Biophysical chemistry: the conformation of biological macromolecules, p. 287–288. W. H. Freeman, San Francisco.
   Google Scholar
• Carter, C. J., M. Cannon, and A. Jiménez. 1980. A trichoder-min-resistant mutant of Saccharomyces cerevisiae with an abnormal distribution of native ribosomal subunits. Eur. J. Bio-chem. 107:173–183.
   Google Scholar
• Cormier, P., H. B. Osborne, J. Morales, T. Bassez, R. Poule, A. Mazabraud, O. Mulner-Lorillon, and R. Belle. 1991. Molecular cloning of Xenopus elongation factor 1γ, major M-phase promoting factor substrate. Nucleic Acids Res. 19:6644.
   PubMedGoogle Scholar
• Couto, J. R., J. Tamm, R. Parker, and C. Guthrie. 1987. A trans-acting suppressor restores splicing of a yeast intron with a branch point mutation. Genes Dev. 1:445–455.
   PubMed Web of Science ®Google Scholar
• Creutz, C. E., S. L. Snyder, and N. G. Kambouris. 1991. Calcium-dependent secretory vesicle-binding and lipid-binding proteins of Saccharomyces cerevisiae. Yeast 7:229–244.
   PubMedGoogle Scholar
• Dasmahapatra, B., L. Skogerson, and K. Chakraburtty. 1981. Purification and properties of elongation factor 1 from Saccharomyces cerevisiae. J. Biol. Chem. 256:10005–10010.
   PubMedGoogle Scholar
• Devereux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387–395.
   PubMed Web of Science ®Google Scholar
• Drain, P., and P. R. Schimmel. 1988. Multiple new genes that determine activity for the first step of leucine biosynthesis in Saccharomyces cerevisiae. Genetics 119:13–20.
   PubMedGoogle Scholar
• Foiani, M., A. M. Cigan, C. J. Paddon, S. Harashima, and A. G. Hinnebusch. 1991. GCD2, a translational repressor of the GCN4 gene, has a general function in the initiation of protein synthesis in Saccharomyces cerevisiae. Mol. Cell. Biol. 11:3203–3216.
   PubMed Web of Science ®Google Scholar
• Girard, J.-P., H. Lehtonen, M. Caizergues-Ferrer, F. Amalric, D. Tollervey, and B. Lapeyre. 1992. GAR1 is an essential small nucleolar RNP protein required for pre-rRNA processing in yeast. EMBO J. 11:673–682.
   PubMed Web of Science ®Google Scholar
• Gonzales, A., A. Jiménez, D. Vázquez, J. E. Davies, and D. Schindler. 1978. Studies on the mode of action of hygromycin B, an inhibitor of translocation in eukaryotes. Biochim. Biophys. Acta 521:459–469.
   PubMedGoogle Scholar
• Gritz, L. R., J. A. Mitlin, M. Cannon, B. Littlewood, C. J. Carter, and J. E. Davies. 1982. Ribosome structure, maturation of ribosomal RNA and drug sensitivity in temperature-sensitive mutants of Saccharomyces cerevisiae. Mol. Gen. Genet. 188: 384–384.
   PubMedGoogle Scholar
• Guthrie, C., H. Nashimoto, and M. Nomura. 1969. Structure and function of E. coli ribosomes. VIII. Cold-sensitive mutants defective in ribosome assembly. Proc. Natl. Acad. Sci. USA 63:384–391.
   PubMed Web of Science ®Google Scholar
• Hadjiolov, A. A.%% 1985. The nucleolus and ribosome biogenesis. Springer-Verlag, New York.
   Google Scholar
• Hughes, J. M. X., and M. Ares, Jr. 1991. Depletion of U3 small nucleolar RNA inhibits cleavage in the 5′ external transcribed spacer of yeast pre-ribosomal RNA and impairs formation of 18S ribosomal RNA. EMBO J. 10:4231–4239.
   PubMed Web of Science ®Google Scholar
• Ito, H., K. Y. Fukuda, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163–168.
   PubMed Web of Science ®Google Scholar
• Janssen, G. M. C., and W. Moller. 1988. Elongation factor 1βγ fromrtemia: purification and properties of its subunits. Eur. J. Biochem. 171:119–129.
   PubMedGoogle Scholar
• Kambouris, N. G., D. J. Burke, and C. E. Creutz. 1993. Cloning and genetic characterization of a calcium- and phospholipid-binding protein from Saccharomyces cerevisiae that is homologous to translation elongation factor-1 γ. Yeast 9:151–163.
   PubMedGoogle Scholar
• Kinzy, T. G., T. L. Ripmaster, and J. L. Woolford, Jr. Submitted for publication.
   Google Scholar
• Kohno, K., T. Fukui, E. Ohtsuka, M. Ikehara, and Y. Okada. 1986. Amino acid sequence of mammalian elongation factor 2 deduced from the cDNA: homology with GTP-binding proteins. Proc. Natl. Acad. Sci. USA 83:4978–4982.
   PubMedGoogle Scholar
• Kumabe, T., Y. Sohma, and T. Yamamoto. 1991. Human cDNAs encoding elongation factor 1γ and the ribosomal protein L19. Nucleic Acids Res. 20:2598.
   Google Scholar
• Kyte, J., and R. F. Doolittle. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105–132.
   PubMed Web of Science ®Google Scholar
• Larkin, J. C., and J. L. Woolford, Jr. 1983. Molecular cloning and analysis of the CRY1 gene: a yeast ribosomal protein gene. Nucleic Acids Res. 11:403–420.
   PubMedGoogle Scholar
• Lee, W. C., D. Zabetakis, and T. Mélèse. 1992. NSR1 is required for pre-rRNA processing and for the proper maintenance of steady-state levels of ribosomal subunits. Mol. Cell. Biol. 12:3865–3871.
   PubMed Web of Science ®Google Scholar
• Li, H. V., J. Zagorski, and M. Fournier. 1990. Depletion of U14 small nuclear RNA (snR128) disrupts production of 18S rRNA in Saccharomyces cerevisiae. Mol. Cell. Biol. 10:1145–1152.
   PubMed Web of Science ®Google Scholar
• Lindahl, L., R. H. Archer, and J. M. Zengel. 1992. A new rRNA processing mutant of Saccharomyces cerevisiae. Nucleic Acids Res. 20:295–301.
   PubMedGoogle Scholar
• Maessen, G. D. F., R. Anions, J. P. Zeelen, and W. Moller. 1987. Primary structure of elongation factor 1γ from Artemia. FEBS Lett. 223:181–186.
   PubMedGoogle Scholar
• Mizushima, S., and M. Nomura. 1970. Assembly mapping of 30S ribosomal proteins from E. coli. Nature (London) 226:1214–1218.
   PubMed Web of Science ®Google Scholar
• Moritz, M., A. G. Paulovich, Y.-F. Tsay, and J. L. Woolford, Jr. 1990. Depletion of yeast ribosomal proteins L16 or rp59 disrupts ribosome assembly. J. Cell Biol. 111:2261–2274.
   PubMedGoogle Scholar
• Moritz, M., B. A. Pulaski, and J. L. Woolford, Jr. 1991. Assembly of 60S ribosomal subunits is perturbed in temperature-sensitive yeast mutants defective in ribosomal protein L16. Mol. Cell. Biol. 11:5681–5692.
   PubMedGoogle Scholar
• Mortimer, R. K., and D. C. Hawthorne. 1966. Genetic mapping in Saccharomyces. Genetics 53:165–173.
   PubMedGoogle Scholar
• Nagata, S., K. Sagashima, Y. Tsunetsugu-Yokota, K. Fujimura, M. Miyazaki, and Y. Kaziro. 1984. Polypeptide chain elongation factor 1α (EF-lα) from yeast: nucleotide sequence of one of the two genes for EF-1α from Saccharomyces cerevisiae. EMBO J. 3:1825–1830.
   PubMedGoogle Scholar
• Nam, H. G., and H. M. Fried. 1986. Effects of progressive depletion of TCM1 or CYH2 mRNA on Saccharomyces cerevisiae ribosomal protein accumulation. Mol. Cell. Biol. 6:1535–1544.
   PubMedGoogle Scholar
• Nierhaus, K. H.%% 1980. Analysis of the assembly and function of the 50S subunit from Eschenchia coli ribosomes by reconstitution, p. 267-294. In G. Chambliss, G. R. Craven, J. Davies, K. Davis, L. Kahan, and M. Nomura (ed.), Ribosomes: structure, function and genetics. University Park Press, Baltimore.
   Google Scholar
• Palade, G. E.%% 1975. Intracellular aspects of the process of protein synthesis. Science 189:347–358.
   PubMed Web of Science ®Google Scholar
• Perentesis, J. P., L. D. Phan, W. B. Gleason, D. C. LaPorte, D. M. Livingston, and J. W. Bodley. 1992. Saccharomyces cerevisiae elongation factor 2. J. Biol. Chem. 267:1190–1197.
   PubMedGoogle Scholar
• Ripmaster, T. L., G. P. Vaughn, and J. L. Woolford, Jr. 1992. A putative ATP-dependent RNA helicase involved in ribosome assembly in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 89:11131–11135.
   PubMedGoogle Scholar
• Rose, M. D., P. Novick, J. H. Thomas, D. Botstein, and G. R. Fink. 1987. A Saccharomyces cerevisiae genomic plasmid based on a centromere containing shuttle vector. Gene 60:237–243.
   PubMed Web of Science ®Google Scholar
• Rudolph, H. K., A. Antebi, G. R. Fink, C. M. Buckley, T. E. Dorman, J. LeVitre, L. S. Davidow, J.-I. Mao, and D. T. Moir. 1988. The yeast secretory pathway is perturbed by mutation in PMR1, a member of a Ca2+ ATPase family. Cell 58:133–145.
   Google Scholar
• Russel, I. D., and D. Tollervey. 1992. NOP3 is an essential yeast protein which is required for pre-rRNA processing. J. Cell Biol. 119:737–747.
   PubMedGoogle Scholar
• Sachs, A. B., and R. W. Davis. 1990. Translation initiation and ribosomal biogenesis: involvement of a putative rRNA helicase and RPL46. Science 247:1077–1079.
   PubMed Web of Science ®Google Scholar
• Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
   Google Scholar
• Sanger, F., S. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463–5467.
   PubMed Web of Science ®Google Scholar
• Saraste, M., P. R. Sibbald, and A. Wittinghofer. 1990. The P-loop: a common motif in ATP- and GTP-binding proteins. Trends Biochem. Sci. 15:430–434.
   PubMed Web of Science ®Google Scholar
• Schirmaier, F., and P. Phillipson. 1984. Identification of two genes coding for the translation elongation factor EF-1α of S. cerevisiae. EMBO J. 3:3311–3315.
   PubMedGoogle Scholar
• Serrano, R., M. C. Kielland-Brandt, and G. R. Fink. 1986. Yeast plasma membrane ATPase is essential for growth and has homology with (Na+ + K+), K+ and Ca2+-ATPases. Nature (London) 319:689–693.
   PubMed Web of Science ®Google Scholar
• Sherman, F., G. R. Fink, and J. B. Hicks. 1986. Methods in yeast genetics, p. 166–167. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
   Google Scholar
• Shuai, K., and J. R. Warner. 1991. A temperature sensitive mutant of Saccharomyces cerevisiae defective in pre-rRNA processing. Nucleic Acids Res. 19:5059–5064.
   PubMedGoogle Scholar
• Sikorski, R. S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122:19–27.
   PubMed Web of Science ®Google Scholar
• Singh, A., and T. R. Manney. 1974. Genetic analysis of mutations affecting growth of Saccharomyces cerevisiae at low temperature. Genetics 77:651–659.
   PubMedGoogle Scholar
• Stern, S., T. Powers, L.-M. Changchien, and H. F. Noller. 1989. RNA-protein interactions in 30S ribosomal subunits: folding and function of 16S rRNA. Science 244:783–790.
   PubMed Web of Science ®Google Scholar
• Surguchov, A. P., E. S. Fominykch, V. N. Smirnov, M. D. Ter-Avanesyan, L. N. Mironova, and S. G. Inge-Vechtomov. 1981. Further characterization of recessive suppression in yeast. Isolation of the low-temperature sensitive mutant of Saccharomyces cerevisiae defective in the assembly of 60S ribosomal subunits. Biochim. Biophys. Acta 654:149–155.
   PubMedGoogle Scholar
• Tai, P.-C., D. P. Kessler, and J. Ingraham. 1969. Cold-sensitive mutations in Salmonella typhimurium which affect ribosome synthesis. J. Bacteriol. 97:1298–1304.
   PubMedGoogle Scholar
• Tollervey, D., H. Lehtoken, M. Carmo-Fonseca, and E. C. Hurt. 1991. The small nucleolar RNP protein NOP1 (fibrillarin) is required for pre-rRNA processing in yeast. EMBO J. 10:573–583.
   PubMed Web of Science ®Google Scholar
• Trapman, J., J. Retel, and R. J. Planta. 1975. Ribosomal precursor particles from yeast. Exp. Cell Res. 90:95–104.
   PubMedGoogle Scholar
• Traub, P., and M. Nomura. 1968. Structure and function of E. coli ribosomes, V. Reconstitution of functionally active 30S ribosomal particles from RNA and proteins. Proc. Natl. Acad. Sci. USA 59:777–784.
   PubMed Web of Science ®Google Scholar
• Udem, S. A., and J. R. Warner. 1973. The cytoplasmic maturation of a ribosomal precursor ribonucleic acid in yeast. J. Biol. Chem. 248:1412–1416.
   PubMed Web of Science ®Google Scholar
• Walderhaug, M. O., R. L. Post, G. Saccomani, R. T. Leonard, and D. P. Briskin. 1985. Structural relatedness of three ion-transport adenosine triphosphatases around their active sites of phosphorylation. J. Biol. Chem. 260:3852–3859.
   PubMedGoogle Scholar
• Warner, J. R., and R. Soeiro. 1967. Nascent ribosomes from HeLa cells. Proc. Natl. Acad. Sci. USA 58:1981–1990.
   Google Scholar
• Wittekind, M., J. M. Kolb, J. Dodd, M. Yamagishi, S. Memet, J.-M. Buhler, and M. Nomura. 1990. Conditional expression of RPA190, the gene encoding the largest subunit of yeast RNA polymerase I: effects of decreased rRNA synthesis on ribosomal protein synthesis. Mol. Cell. Biol. 10:2049–2059.
   PubMedGoogle Scholar
• Woolford, J. L., Jr. 1991. The structure and biogenesis of yeast ribosomes. Adv. Genet. 29:63–118.
   PubMedGoogle Scholar
• Woolford, J. L., Jr., and J. R. Warner. 1991. The ribosome and its synthesis, p. 587–626. In J. Broach, E. Jones, and J. Pringle (ed.), The molecular biology of the yeast Saccharomyces cerevisiae. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
   Google Scholar
• Yoon, H., and T. F. Donahue. 1992. The sui1 suppressor locus in Saccharomyces cerevisiae encodes a translation factor that functions during tRNAiMet recognition of the start codon. Mol. Cell. Biol. 12:248–260.
   PubMed Web of Science ®Google Scholar