Transcription Termination

References

• Bremer H., Konrad M. A complex of enzymatically synthesized RNA and template DNA. Proc. Natl. Acad. Sci., U.S.A. 1964; 51: 801
   Google Scholar
• Richardson J. P. Enzymic synthesis of RNA from T7 DNA. J. Mol. Biol. 1966; 21: 115
   Google Scholar
• Scott M. P. Molecules and puzzles from the antennapedia homeotic gene complex of Drosophila. Trends in Genetics 1985; 1: 74
   Google Scholar
• von Hippel P. H., Yager T. D. Transcription elongation and termination are competitive kinetic processes. Proc. Natl. Acad. Sci. U.S.A. 1991; 88: 2307
   PubMedGoogle Scholar
• Burgess R. R., Travers A. A., Dunn J. J., Bautz E. K. F. Factor stimulating transcription by RNA polymerase. Nature 1969; 221: 43
   PubMed Web of Science ®Google Scholar
• Chamberlin M. J. RNA polymerase — an overview. RNA Polymerase, R. Losick, M. Chamberlin. Cold Spring Harbor Laboratory, Cold Spring Harbor 1976; 17
   Google Scholar
• Metzger W., Schickor P., Heumann H. A cinematographic view of Escherichia coli RNA polymerase translocation. EMBO J. 1989; 8: 2745
   Google Scholar
• Krummel B., Chamberlin M. J. Structural analysis of ternary complexes of Escherichia coli RNA pholymerase. Deoxyribonuclease I footprinting of defined complexes. J. Mol. Biol. 1992; 225: 239
   PubMed Web of Science ®Google Scholar
• Gamper H. B., Hearst J. E. A topological model for transcription based on unwinding angle analysis of E. coli RNA polymerase binary, initiation and ternary complexes. Cell 1982; 29: 81
   PubMed Web of Science ®Google Scholar
• Rice G. A., Kane C. M., Chamberlin M. J. Footprinting analysis of mammalian RNA polymerase II along its transcript: an alternative view of transcription elongation. Proc. Natl. Acad. Sci. U.S.A. 1991; 88: 4245
   PubMed Web of Science ®Google Scholar
• Kainz M., Roberts J. Structure of transcription elongation complexes in vivo. Science 1992; 255: 838
   PubMedGoogle Scholar
• Richardson J. P. Attachment of nascent RNA molecules to superhelical DNA. J. Mol. Biol. 1975; 98: 565
   PubMed Web of Science ®Google Scholar
• Surratt C. K., Milan S. C., Chamberlin M. J. Spontaneous cleavage of RNA in ternary complexes of Escherichia coli RNA polymerase and its significance for the mechanism of transcription. Proc. Natl. Acad. Sci. U.S.A. 1991; 88: 7983
   PubMedGoogle Scholar
• Liu L. F., Wang J. C. Supercoiling of the DNA template during transcription. Proc. Natl. Acad. Sci. U.S.A. 1987; 84: 7024
   PubMed Web of Science ®Google Scholar
• Drlica K. Biology of bacterial deoxyribonucleic acid topoisomerases. Microbiol. Rev. 1984; 48: 273
   PubMedGoogle Scholar
• Davis R. W., Hyman R. Physical locations of the in vitro RNA initiation site and termination sites of T7M DNA. Cold Spring Harbor Symp. Quant. Biol. 1970; 35: 269
   Google Scholar
• Yager T. D., von Hippel P. H. Transcript Elongation and Termination in Escherichia Coli. Escherichia Coli and Salmonella Typhimurium, F. C. Neidhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter, H. E. Umbarger. American Society for Microbiology, Washington, D.C. 1987; 1241
   Google Scholar
• Mosteller R. D., Yanofsky C. Transcription of the tryptophan operon in Escherichia coli: rifampicin as an inhibitor of initiation. J. Mol. Biol. 1970; 48: 525
   PubMed Web of Science ®Google Scholar
• Gotta S. L., Miller O. L., Jr., French S. L. rRNA transcription rate in Escherichia coli. J. Bacteriol. 1991; 173: 6647
   PubMed Web of Science ®Google Scholar
• Maizels N. The nucleotide sequence of the lactose messenger ribonucleic acid transcribed from the UV5 promoter mutant of E. coli. Proc. Natl. Acad. Sci. U.S.A. 1973; 70: 3585
   PubMed Web of Science ®Google Scholar
• Darlix J. L., Fromageot F. Discontinuous in vitro transcription of DNA. Biochimie 1972; 54: 47
   Google Scholar
• Rosenberg M., Court D., Shimatake H., Brady C., Wulff D. L. The relationship between function and DNA sequence in an intercistronic regulatory region in phage γ. Nature 1978; 272: 414
   PubMedGoogle Scholar
• Landick R., Yanofsky C. Stability of an RNA secondary structure affects in vitro transcription pausing in the trp operon leader region. J. Biol. Chem. 1984; 259: 11550
   PubMed Web of Science ®Google Scholar
• Morgan W. D., Bear D. G., von Hippel P. H. Rho-dependent termination of transcription. II. Kinetics of mRNA elongation during transcription from the bacteriophage γ PR promoter. J. Biol. Chem. 1983; 258: 9565
   PubMedGoogle Scholar
• Lee D. N., Phung L., Stewart J., Landick R. Transcription pausing by Escherichia coli RNA polymerase is modulated by downstream DNA sequences. J. Biol. Chem. 1990; 265: 15145
   Google Scholar
• Levin J. R., Chamberlin M. J. Mapping and characterization of transcriptional pause sites in the early genetic region of bacteriophage T7. J. Mol. Biol 1987; 196: 61
   PubMedGoogle Scholar
• Chan C. L., Landick R. The Salmonella typhimurium his operon leader region contains an RNA hairpin-dependent transcription pause site. J. Biol. Chem. 1989; 264: 20796
   PubMed Web of Science ®Google Scholar
• Kerppola T. K., Kane C. M. Analysis of the signals for transcription termination by purified RNA polymerase II. Biochemistry 1990; 29: 269
   PubMedGoogle Scholar
• Ishii S., Ihara M., Maekawa T., Nakamura Y., Uchida H., Imamoto F. The nucleotide sequence of the cloned nusA gene and its flanking region of Escherichia coli. Nucleic Acids Res. 1984; 12: 3333
   PubMedGoogle Scholar
• Kassavetis G. A., Chamberlin M. J. Pausing and termination of transcription within the early region of bacteriophage T7 DNA in vitro. J. Biol. Chem. 1981; 256: 2777
   PubMed Web of Science ®Google Scholar
• Kingston R. E., Chamberlin M. J. Pausing and attenuation of in vitro transcription in the rrnB operon of E. coli. Cell 1981; 27: 523
   PubMedGoogle Scholar
• Fisher R., Yanofsky C. A complementary DNA oligomer releases a transcription pause complex. J. Biol. Chem. 1983; 258: 9208
   PubMed Web of Science ®Google Scholar
• Lau L. F., Roberts J. W., Wu R. RNA polymerase pausing and transcript release at the λtR1 terminator in vitro. J. Biol. Chem. 1983; 258: 9391
   PubMedGoogle Scholar
• Schmidt M. C., Chamberlin M. J. Amplification and isolation of Escherichia colinus A protein and studies of its effects on in vitro RNA chain elongation. Biochemistry 1984; 23: 197
   Google Scholar
• Greenblatt J., Li J. Interaction of the sigma factor and the nusA gene protein of E. coli with RNA polymerase in the initiation-termination cycle of transcription. Cell 1981; 24: 421
   PubMed Web of Science ®Google Scholar
• Gill S. C., Weitzel S. E., von Hippel P. H. Escherichia coli s70 and nusA proteins. I. Binding interactions with core RNA polymerase in solution and within the transcription complex. J. Mol. Biol. 1991; 220: 307
   PubMed Web of Science ®Google Scholar
• Landick R., Yanofsky C. Isolation and structural analysis of the Escherichia coli trp leader paused transcription complex. J. Mol. Biol. 1987; 196: 363
   PubMed Web of Science ®Google Scholar
• Dissinger S., Hanna M. M. RNA-protein interactions in a NusA-containing Escherichia coli transcription complex paused at an RNA hairpin. J. Mol. Biol. 1991; 219: 11
   Google Scholar
• Faus I., Chen C.-Y. A., Richardson J. P. Sequences in the 5′ proximal segment of the paused transcript affect NusA-mediated enhancement of transcriptional pausing. J. Biol. Chem. 1988; 263: 10830
   Google Scholar
• Craven M. G., Friedman D. I. Analysis of the Escherichia coli nusA 10(Cs) allele: relating nucleotide changes to phenotypes. J. Bacteriol. 1991; 173: 1485
   Google Scholar
• Greenblatt J., Li J., Adhya S., Friedman D. I., Baron L. S., Redfield B., Kung H-F., Weissbach H. L factor that is required for β-galactosidase synthesis is the nusA gene product involved in transcription. Proc. Natl. Acad. Sci. U.S.A. 1980; 77: 1991
   Google Scholar
• Kung H.-F., Spears C., Weissbach H. Purification and properties of a soluble factor required for the deoxyribonucleic acid-directed in vitro synthesis of β-galactosidase. J. Biol. Chem. 1975; 250: 1556
   Google Scholar
• Ruteshouser E. C., Richardson J. P. Identification and characterization of transcription termination sites in the Escherichia coli lacZ gene. J. Mol. Biol. 1989; 208: 23
   PubMed Web of Science ®Google Scholar
• Landick R., Carey J., Yanofsky C. Translation activates the paused transcription complex and restores transcription of the trp operon leader region. Proc. Natl. Acad. Sci. U.S.A. 1985; 82: 4663
   PubMed Web of Science ®Google Scholar
• Freidman D. J., Gottesman M. Lytic Mode of Lambda Development, I I Lambda, R. W. Hendrix, J. W. Roberts, F. W. Stahl, R. A. Weisberg. Cold Spring Harbor Laboratory, Cold Spring Harbor 1983
   Google Scholar
• Natori S. Stimulatory proteins of RNA polymerase II from Ehrlich ascites tumor cells. Mol. Cell. Biochem. 1982; 46: 173
   Google Scholar
• Reinberg D., Roeder R. G. Factors involved in specific transcription by mammalian RNA polymerase II. Transcription factor IIS stimulates elongation of RNA chains. J. Biol. Chem. 1987; 262: 3331
   PubMed Web of Science ®Google Scholar
• Reines D., Chamberlin M. J., Kane C. M. Transcription elongation factor SH (TFIIS) enables RNA polymerase II to elongate through a block to transcription in a human gene in vitro. J. Biol. Chem. 1989; 264: 10799
   PubMed Web of Science ®Google Scholar
• Siva Raman L., Reines D., Kane C. M. Purified elongation factor SII is sufficient to promote read-through by purified RNA polymerase II at specific termination sites in the human histone H3.3 gene. J. Biol. Chem. 1990; 265: 14554
   Google Scholar
• Sluder A. E., Greenleaf A. L., Price D. H. Properties of a Drosophila RNA polymerase II elongation factor. J. Biol. Chem. 1989; 264: 8963
   PubMedGoogle Scholar
• Sawadago M., Huet J., Fromageot P. Similar binding sites for P37 factor on yeast RNA polymerases A and B. Biochem. Biophys. Res. Commun. 1980; 96: 258
   Google Scholar
• Reines D. Elongation factor-dependent transcript shortening by template-engaged RNA polymerase II. J. Biol. Chem. 1992; 267: 3795
   PubMedGoogle Scholar
• Reines D., Ghanouni P., Li Q., Mote J., Jr. The RNA polymerase II elongation factor-dependent involves nascent RNA cleavage. J. Bio. Chem. 1992; 267: 15516
   PubMed Web of Science ®Google Scholar
• Izban M. G., Luse D. S. The RNA polymerase II ternary complex cleaves the nascent transcript in a 3′ 5′ direction in the presence of elongation factor SII. Genes Dev. 1992; 6: 1342
   PubMed Web of Science ®Google Scholar
• Hirashima S., Hirai H., Nakanishi Y., Natori S. Molecular cloning and characterization of cDNA for eukaryotic transcription factor S-II. J. Biol. Chem. 1988; 263: 3858
   PubMedGoogle Scholar
• Marshall T. K., Guo H., Price D. H. Drosophila RNA polymerase II elongation factor Dm-SII has homology to mouse S-II and sequence similarity to yeast PPR2. Nucleic Acids Res. 1990; 18: 6293
   PubMedGoogle Scholar
• Yoo O.-J., Yoon H-S., Baek K. H., Jeon C-J., Miyamoto K., Ueno A., Agarwal K. Cloning, expression and characterization of the human transcription elongation factor, TFIIS. Nucleic Acids Res. 1991; 19: 1073
   PubMedGoogle Scholar
• Chen H. C., England L., Kane C. M. Characterization of a HeLa cDNA clone for the human SII protein, an elongation factor for RNA polymerase II. Gene 1992; 116: 253
   Google Scholar
• Kipling D., Kearsey S. E. TFIIS and strandtransfer proteins. Nature 1991; 353: 509
   PubMedGoogle Scholar
• Bengal E., Flores O., Krauskopf A., Reinberg D., Aloni Y. Role of the mammalian transcription factors IIF, IIS, and IIX during elongation by RNA polymerase II. Mol. Cell. Biol. 1991; 11: 1195
   PubMedGoogle Scholar
• Izban M. G., Luse D. S. Factor-stimulated RNA polymerase II transcribes at physiological elongation rates on naked DNA but very poorly on chromatin templates. J. Biol. Chem. 1992; 267: 13647
   PubMed Web of Science ®Google Scholar
• Flores O., Maldonado E., Reinberg D. Factors involved in specific transcription by mammalian RNA polymerase. II. Factors HE and IIF independently interact with RNA polymerase II. J. Biol. Chem. 1989; 264: 8913
   PubMedGoogle Scholar
• Sopta M., Carthew R. W., Greenblatt J. Isolation of three proteins that bind to mammalian RNA polymerase II. J. Biol. Chem. 1985; 260: 10353
   PubMedGoogle Scholar
• Cozzarelli N. R., Gerrard S. P., Schlissel M., Brown D. D., Bogenhagen D. F. Purified RNA polymerase III accurately and efficiently terminates transcription of 5S RNA genes. Cell 1983; 34: 829
   PubMed Web of Science ®Google Scholar
• Jeng S.-T., Gardner J. F., Gumport R. I. Transcription termination by bacteriophage T7 RNA polymerase at rho-independent terminators. J. Biol. Chem. 1990; 265: 3823
   PubMed Web of Science ®Google Scholar
• Dedrick R. L., Kane C. M., Chamberlin M. J. Purified RNA polymerase II recognizes specific termination sites during transcription in vitro. J. Biol. Chem. 1987; 262: 9098
   PubMedGoogle Scholar
• Kerppola T. K., Kane C. M. Intrinsic sites of transcription termination and pausing of the c-myc gene. Mol. Cell. Biol. 1988; 8: 4389
   PubMedGoogle Scholar
• Rosenberg M., Court D. Regulatory sequences involved in the promotion and termination of RNA transcription. Annu. Rev. Genet. 1979; 13: 319
   PubMed Web of Science ®Google Scholar
• Brendel V., Hamm G. H., Trifonov E. N. Terminators of transcription with RNA polymerase from Escherichia coli: what they look like and how to find them. J. Biolmol. Struct. Dyn. 1986; 3: 705
   PubMed Web of Science ®Google Scholar
• Carafa Y. D., Brody E., Thermes C. Prediction of rho-independent Escherichia coli transcription terminators: a statistical analysis of their RNA stem-loop structures. J. Mol. Biol 1990; 216: 835
   Google Scholar
• Telesnitsky A., Chamberlin M. J. Terminator-distal sequences determine the in vitro efficiency of the early terminators of bacteriophages T3 and T7. Biochemistry 1989; 28: 5210
   Google Scholar
• Lynn S. P., Kasper L. M., Gardner J. F. Contributions of RNA secondary structure and length of the thymidine tract to transcription termination at the thr operon attenuator. J. Biol. Chem. 1988; 263: 472
   Google Scholar
• Cheng S.-W. C., Lynch E. C., Leason K. R., Court D. L., Shapiro B. A., Friedman D. I. Functional importance of sequence in the stem-loop of a transcription terminator. Science 1991; 254: 1205
   Google Scholar
• Ryan T., Chamberlin M. J. Transcription analyses with heteroduplex trp attenuator templates indicate that the transcript stem and loop structure serves as the termination signal. J. Biol. Chem. 1983; 258: 4690
   PubMedGoogle Scholar
• Yang M. T., Gardner J. F. Transcription termination directed by heteroduplex thr attenuator templates. Evidence that the transcript stem and loop structure is the termination signal. J. Biol. Chem. 1989; 264: 2634
   Google Scholar
• Tuerk C., Gauss P., Thermes C., Groebe D. R., Gayle M., Guild N., Stormo G., d'Aubenton-Carafa Y., Uhlenbeck O. C., Tinoco I., Jr., Brody E. N., Gold L. CUUCGG hairpins: extraordinarily stable RNA secondary structures associated with various biochemical processes. Proc. Natl. Acad. Sci. U.S.A. 1988; 85: 1364
   PubMed Web of Science ®Google Scholar
• Arndt K. M., Chamberlin M. J. RNA chain elongation by Escherichia coli RNA polymerase: factors affecting the stability of elongating ternary complexes. J. Mol. Biol. 1990; 213: 79
   PubMed Web of Science ®Google Scholar
• Martin F. H., Tinoco I. J. DNA-RNA hybrid duplexes containing oligo(dA:rU) sequences are exceptionally unstable and may facilitate termination of transcription. Nucleic Acids Res. 1980; 8: 2295
   PubMed Web of Science ®Google Scholar
• Reynolds R., Chamberlin M. J. Parameters affecting transcription termination by Escherichia coli RNA. II. Construction and analysis of hybrid terminators. J. Mol. Biol. 1992; 224: 53
   PubMedGoogle Scholar
• Farnham P. J., Platt T. A model for transcription termination suggested by studies on the trp attenuator in vitro using base analogs. Cell 1980; 20: 739
   PubMed Web of Science ®Google Scholar
• Reynolds R., Bermudez-Cruz R. M., Chamberlin M. J. Parameters affecting transcription termination by Escherichia coli RNA polymerase. I. Analysis of 13 rho-independent terminators. J. Mol. Biol 1992; 224: 31
   PubMedGoogle Scholar
• Andrews C. A., Richardson J. P. Transcription termination factor rho mediates simultaneous release of RNA transcripts and DNA template from complexes with Escherichia coli RNA polymerase. J. Biol. Chem. 1985; 260: 5826
   PubMed Web of Science ®Google Scholar
• Arndt K. M., Chamberlin M. J. Transcription termination in Escherichia coli: measurement of the rate of enzyme release from rho-dependent terminators. J. Mol. Biol. 1988; 202: 271
   Google Scholar
• Hinkle D. C., Chamberlin M. J. Studies of the binding of Escherichia coli RNA polymerase to DNA I. The role of sigma subunit in site selection. J. Mol. Biol. 1972; 70: 157
   PubMed Web of Science ®Google Scholar
• Roberts J. W. Termination factor for RNA synthesis. Nature (London) 1969; 224: 1168
   PubMed Web of Science ®Google Scholar
• Bartsch I., Schoneberg C., Grummt I. Purification and characterization of TTFI, a factor that mediates termination of mouse ribosomal DNA transcription. Mol. Cell. Biol. 1988; 8: 3891
   PubMedGoogle Scholar
• Shuman S., Broyles S., Moss B. Purification and characterization of a transcription termination factor from vaccinia virions. J. Biol. Chem. 1987; 262: 12372
   PubMedGoogle Scholar
• Richardson J. P. Rho-dependent transcription termination. Biochim. Biophys. Acta 1990; 1048: 127
   PubMedGoogle Scholar
• Galluppi G. R., Richardson J. P. ATP-induced changes in the binding of RNA synthesis termination protein rho to RNA. J. Mol. Biol. 1980; 138: 513
   PubMed Web of Science ®Google Scholar
• Richardson J. P., Conaway R. RNA release activity of transcription termination protein is dependent on the hydrolysis of nucleoside triphosphates. Biochemistry 1980; 19: 4293
   Google Scholar
• Richardson L. V., Richardson J. P., unpublished experiments
   Google Scholar
• Alifano P., Rivellini F., Limauro D., Bruni C. B., Carlomagno M. S. A consensus motif common to all rho-dependent prokaryotic transcription terminators. Cell 1991; 64: 553
   PubMed Web of Science ®Google Scholar
• Lowery C., Richardson J. P. Characterization of the nucleoside triphosphate phosphohydrolase (ATPase) activity of RNA synthesis termination factor: II. Influence of synthetic RNA homopolymers and random copolymers on the reaction. J. Biol. Chem. 1977; 252: 1381
   PubMedGoogle Scholar
• Finger L. R., Richardson J. P. Stabilization of the hexameric form of Escherichia coli protein rho under ATP hydrolysis conditions. J. Mol. Biol. 1982; 156: 203
   Google Scholar
• Pinkham J. L., Platt T. Nucleotide sequence of the E. coli rho gene and its regulatory regions. Nucleic Acids Res. 1983; 11: 3531
   PubMedGoogle Scholar
• Bear D. G., Hicks P. S., Escudero K. W., Andrews C. L., McSwiggen J. A., von Hippel P. H. Interactions of Escherichia coli transcription termination factor rho with RNA. J. Mol. Biol. 1988; 199: 623
   PubMed Web of Science ®Google Scholar
• Geiselmann J., Seifried S. E., Yager T. D., Liang C., von Hippel P. H. Physical properties of the E. coli transcription termination factor rho. II. Quaternary structure of the rho hexamer. Biochemistry 1992; 31: 121
   Google Scholar
• Dombroski A. J., Platt T. Structure of rho factor: An RNA-binding domain and a separate region with strong similarity to proven ATP-binding domains. Proc. Natl. Acad. Sci. U.S.A. 1988; 85: 2538
   PubMed Web of Science ®Google Scholar
• Dolan J. W., Marshall N. F., Richardson J. P. Transcription termination factor rho has three distinct structural domains. J. Biol. Chem. 1990; 265: 5747
   PubMed Web of Science ®Google Scholar
• Geiselmann J., Yager T. D., von Hippel P. H. Functional interactions of ligand cofactors with E. coli transcription termination factor rho: II. Binding of RNA. Protein Science 1992; 1: 861
   Google Scholar
• Stitt B. L. Escherichia coli transcription termination protein rho has three hydrolytic sites for ATP. J. Biol. Chem. 1988; 263: 111
   Google Scholar
• Geiselmann J., von Hippel P. H. Functional interactions of ligand cofactors with E. coli transcription termination factor rho: I. Binding of ATP. Protein Science 1992; 1: 850
   Google Scholar
• Brennan C. A., Dombroski A. J., Platt T. Transcription termination factor rho is an RNA-DNA helicase. Cell 1987; 48: 945
   PubMed Web of Science ®Google Scholar
• Platt T., Richardson J. P. E. coli rho factor: protein and enzyme of transcription termination. Transcriptional Regulation, S. L. McKnight, K. R. Yamarnoto. Cold Spring Harbor Press, Cold Spring Harbor 1992
   Google Scholar
• Jin D. J., Burgess R. R., Richardson J. P., Gross C. A. Termination efficiency at rho-dependent terminators depends on kinetic coupling between RNA polymerase and rho. Proc. Natl. Acad. Sci. U.S.A. 1992; 89: 1453
   PubMed Web of Science ®Google Scholar
• Richardson J. P. Preventing the synthesis of unused transcripts by rho factor. Cell 1991; 64: 1047
   PubMed Web of Science ®Google Scholar
• Li S. C., Squires C. L., Squires C. Anti-termination of E. coli rRNA transcription is caused by a control region segment containing lambda nut-like sequences. Cell 1984; 38: 851
   PubMed Web of Science ®Google Scholar
• Aksoy S., Squires C. L., Squires C. Evidence for Antitermination in Escherichia coli rRNA transcription. J. Bacteriol 1984; 159: 260
   PubMed Web of Science ®Google Scholar
• Grummt I., Maier U., Öhrlein A., Hassouna N., Bachellerie J.-P. Transcription of mouse rDNA terminates downstream of the 3′ end of 28S RNA and involves the interaction of factors with repeated sequences in the 3′ spacer. Cell 1985; 43: 801
   PubMedGoogle Scholar
• Kuhn A., Bartsch I., Grummt I. Specific interaction of the murine transcription termination factor TTF I with class-I RNA polymerases. Nature 1990; 344: 559
   PubMedGoogle Scholar
• Christianson T. W., Clayton D. A tridecamer DNA sequence supports human mitochondrial RNA 3′ end formation in vitro. Mol. Cell Biol. 1988; 8: 4502
   PubMedGoogle Scholar
• Hess J. F., Parisi M. A., Bennett J. L., Clayton D. A. Impairment of mitochondrial transcription termination by a point mutation associated with the MELAS subgroup of mitochondrial encephalomyopathies. Nature 1991; 351: 236
   PubMed Web of Science ®Google Scholar
• Kruse G., Narasimhan N., Attardi G. Termination of transcription in human mitochondria: identification and purification of a DNA binding protein factor that promotes termination. Cell 1989; 58: 391
   PubMed Web of Science ®Google Scholar
• Pavco P. A., Steege D. A. Elongation by E. coli RNA polymerase is blocked in vitro by a site-specific DNA binding protein. J. Biol. Chem. 1990; 265: 9960
   PubMedGoogle Scholar
• Connelly S., Manley J. L. RNA polymerase II transcription termination is mediated specifically by protein binding to a CCAAT box sequence. Mol. Cell. Biol 1989; 9: 5254
   PubMedGoogle Scholar
• Rohrmann G., Yuen L., Moss B. Transcription of vaccinia virus early genes by enzymes isolated from vaccinia virions terminates downstream of a regulatory sequence. Cell 1986; 46: 1029
   PubMedGoogle Scholar
• Luo Y., Hagler J., Shuman S. Discrete functional stages of vaccinia virus early transcription during a single round of RNA synthesis in vitro. J. Biol. Chem. 1991; 266: 13303
   PubMed Web of Science ®Google Scholar
• Shuman S., Moss B. Factor-dependent transcription termination by vaccinia virus RNA polymerase. J. Biol. Chem. 1988; 263: 6220
   PubMedGoogle Scholar
• Hagler J., Shuman S. A freeze-frame view of eukaryotic transcription during elongation and capping of nascent mRNA. Science 1992; 255: 983
   PubMed Web of Science ®Google Scholar
• Schmidt M. C., Chamberlin M. J. nusA protein of Escherichia coli is an efficient transcription termination factor for certain terminator sites. J. Mol. Biol. 1987; 195: 809
   PubMed Web of Science ®Google Scholar
• Gottlieb E., Steitz J. A. Function of the mammalian La protein: evidence for its action in transcription termination by RNA polymerase III. EMBO J. 1989; 8: 851
   PubMed Web of Science ®Google Scholar
• Briat J.-F., Chamberlin M. J. Identification and characterization of a new transcriptional termination factor from Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 1984; 81: 7373
   PubMedGoogle Scholar
• Sullivan S. L., Gottesman M. E. Requirement for E. coli NusG protein in factor-dependent transcription termination. Cell 1992; 68: 989
   PubMed Web of Science ®Google Scholar
• Zengel J. M., Lindahl L. Ribosomal protein L4 stimulates in vitro termination of transcription at a nusA-dependent terminator in the S10 operon leader. Proc. Natl. Acad. Sci. U.S.A. 1990; 87: 2675
   PubMed Web of Science ®Google Scholar
• Lau L., Roberts J. W., Wu R. Transcription terminates at λtR, in three clusters. Proc. Natl. Acad. Sci. U.S.A. 1982; 79: 6171
   PubMedGoogle Scholar
• Sigmund C. D., Morgan E. A. NusA protein affects transcriptional pausing and termination in vitro by binding to different sites on the transcription complex. Biochemistry 1988; 27: 5622
   PubMed Web of Science ®Google Scholar
• Farnham P. J., Greenblatt J., Platt T. Effects of NusA protein on transcription termination in the tryptophan operon of Escherichia coli. Cell 1982; 29: 945
   PubMed Web of Science ®Google Scholar
• Schmidt M. C., Chamberlin M. J. Binding of rho factor to Escherichia coli RNA polymerase mediated by nusA protein. J. Biol. Chem. 1984; 259: 15000
   PubMed Web of Science ®Google Scholar
• Li J., Horwitz R., McCracken S., Greenblatt J. NusG, a new Escherichia coli elongation factor involved in transcriptional antitermination by the N protein of phage λ. J. Biol. Chem. 1992; 267: 6012
   PubMedGoogle Scholar
• Linn T., Greenblatt J. The NusA and NusG proteins of Escherichia coli increase the in vitro read-through frequency of a transcriptional attenuator preceding the gene for the β subunit of RNA polymerase. J. Biol. Chem. 1992; 267: 1449
   PubMed Web of Science ®Google Scholar
• Rinke J., Steitz J. A. Precursor molecules of both human 5S ribosomal RNA and transfer RNAs are bound by a cellular protein reactive with anti-La lupus antibodies. Cell 1982; 29: 149
   PubMed Web of Science ®Google Scholar
• Bachmann M., Pfeifer K., Schröder H.-C., Müller W. E. G. Characterization of the autoantigen La as a nucleic acid-dependent ATPase/dATPase with melting properties. Cell 1990; 60: 85
   PubMed Web of Science ®Google Scholar
• Landick R., Yanofsky C. Transcription Attenuation. Escherichia coli and Salmonella Typhimurium, F. C. Neidhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter, H. E. Umbarger. American Society for Microbiology, Washington, DC 1987; 1276
   Google Scholar
• Roberts J. W. Phage lambda and the regulation of transcription termination. Cell 1988; 52: 5
   PubMedGoogle Scholar
• Turnbough C. L., Hicks K. L., Donahue J. P. Attenuation control of pyrB1 expression in Escherichia coli K-12. Proc. Natl. Acad. U.S.A. 1983; 80: 368
   PubMedGoogle Scholar
• Stewart V., Yanofsky C. Evidence for transcription antitermination control of tryptophanase gene expression in Escherichia coli K-12. J. Bacteriol. 1985; 164: 731
   Google Scholar
• Stewart V., Landick R., Yanofsky C. Rho-dependent transcription termination in the tryptophanase operon leader region of Escherichia coli K-12. J. Bacteriol. 1986; 166: 217
   PubMed Web of Science ®Google Scholar
• Gollnick P., Yanofsky C. tRNATrp translation of leader peptide codon 12 and other factors that regulate expression of the tryptophanase operon. J. Bacteriol. 1990; 172: 3100
   Google Scholar
• Barik S., Bhattacharya P., Das A. Autogenous regulation of transcription termination factor rho. J. Mol. Biol. 1985; 182: 495
   Google Scholar
• Matsumoto Y., Shigesada K., Hirano M., Imai M. Autogenous regulation of the gene for transcription termination factor rho in Escherichia coli: localization and function of its attenuators. J. Bacteriol. 1986; 166: 945
   PubMedGoogle Scholar
• Grayhack E. J., Roberts J. W. Purification of the bacteriophage λ late gene regulator encoded by gene Q. J. Biol. Chem. 1983; 258: 9192
   Google Scholar
• Grayhack E. J., Yang W., Lau L. F., Roberts J. W. Phage lambda gene Q antiterminator recognizes RNA polymerase near the promoter and accelerates it through a pause site. Cell 1985; 42: 259
   PubMed Web of Science ®Google Scholar
• Yarnell W. S., Roberts J. W. The phage λ gene Q transcription antiterminator binds DNA in the late gene promoter as it modifies RNA polymerase. Cell 1992; 69: 1181
   PubMedGoogle Scholar
• Yang X., Hart C. M., Grayhack E. J., Roberts J. W. Transcription antitermination by phage λ gene Q protein requires a DNA segment spanning the RNA start site. Genes Dev. 1987; 1: 217
   PubMedGoogle Scholar
• Mason S. W., Greenblatt J. Assembly of transcription elongation complexes containing the N protein of phage λ and the Escherichia coli elongation factors NusA, NusB, NusG, and S10. Genes Dev. 1991; 5: 1504
   PubMed Web of Science ®Google Scholar
• Barik S., Ghosh B., Whalen W., Lazinski D., Das A. An antitermination protein engages the enlongating transcription apparatus at a promoter-proximal recognition site. Cell 1987; 50: 885
   PubMedGoogle Scholar
• Lazinski D., Grzadzielska E., Das A. Sequence-specific recognition of RNA hairpins by bacteriophage antiterminators requires a conserved arginine-rich motif. Cell 1989; 59: 207
   PubMed Web of Science ®Google Scholar
• Nodwell J. R., Greenblatt J. The nut site of bacteriophage λ is made of RNA and is bound by transcription antitermination factors on the surface of RNA polymerase. Genes Dev. 1991; 5: 2141
   PubMed Web of Science ®Google Scholar
• Yang X., Roberts J. W. Gene Q antiterminator proteins of Escherichia coli phages 82 and λ suppress pausing by RNA polymerase at a dependent terminator and at other sites. Proc. Natl. Acad. Sci. U.S.A. 1989; 86: 5301
   PubMedGoogle Scholar
• Faus I., Richardson J. P. Structural and functional properties of the segments of λ cro mRN A that interact with transcription termination factor rho. J. Mol. Biol. 1990; 212: 53
   Google Scholar
• Chen C.-Y. A., Galluppi G. R., Richardson J. P. Transcription termination at rR1 is mediated by interaction of rho with specific single-stranded domains near the 3′ end of cro mRNA. Cell 1986; 46: 1023
   PubMed Web of Science ®Google Scholar
• Telesnitsky A. P. W., Chamberlin M. J. Sequences linked to prokaryotic promoters can affect the efficiency of downstream termination sites. J. Mol. Biol. 1989; 205: 315
   Google Scholar
• Goliger J. A., Roberts J. W. Sequences required for antitermination by phage 82 Q protein. J. Mol. Biol. 1989; 210: 461
   Google Scholar
• Morgan E. A. Insertions of Tn10 into an E. coli ribosomal RNA operon are incompletely polar. Cell 1980; 21: 257
   Google Scholar
• Berg K. L., Squires C., Squires C. L. Ribosomal RNA operon antitermination: function of leader and spacer region box B-box A sequences and their conservation in diverse microorganisms. J. Mol. Biol. 1989; 209: 345
   PubMed Web of Science ®Google Scholar
• Nodwell J., Greenblatt J. A heterodimer of NusB and S10 binds to the boxA sequence RNA of the rrnG ribosomal RNA operon of E. coli. J. Cell Biochem. 1992; 16E: 185
   Google Scholar
• Sharrock R. A., Course R. L., Nomura M. Defective antitermination of rRNA transcription and derepression of rRNA and tRNA synthesis in the nusB5 mutant of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 1985; 82: 5275
   Google Scholar
• Mahadevan S., Wright A. A bacterial gene involved in transcription antitermination: regulation at a rho-independent terminator in the bgl operon of E. coli. Cell 1987; 50: 485
   Google Scholar
• Houman F., Diaz-Torres M. R., Wright A. Transcriptional antitermination in the bgl operon of E. coli is modulated by a specific RNA binding protein. Cell 1990; 62: 1153
   PubMedGoogle Scholar
• Amster-Choder O., Houman F., Wright A. Protein phosphorylation regulates transcription of the β-glucoside utilization operon in E. coli. Cell 1989; 58: 847
   Google Scholar
• Amster-Choder O., Diaz-Torres M., Wright A. Modulation of the dimerization of a transcriptional antiterminator protein by phosphorylation. Science 1992; 257: 1395
   Google Scholar
• Linderoth N. A., Calendar R. L. The Psu protein of bacteriophage P4 is an antitermination factor for rho-dependent transcription termination. J. Bacteriol. 1991; 173: 6722
   Google Scholar
• Kerppola T. K., Kane C. M. RNA polymerase: regulation of transcript elongation and termination. FASEB J. 1991; 5: 2833
   PubMed Web of Science ®Google Scholar
• Rougvie A. E., Lis J. T. The RNA polymerase II molecule at the 5′ end of the uninduced hsp70 gene of D. melanogaster is transcriptionally engaged. Cell 1988; 54: 795
   PubMed Web of Science ®Google Scholar
• Lee H., Kraus K. W., Wolfner M. F., Lis J. T. DNA sequence requirements for generating paused polymerase at the start of hsp70. Genes Dev. 1992; 6: 284
   PubMedGoogle Scholar
• Kao S.-Y., Caiman A. F., Luciw P. A., Peterlin B. M. Anti-termination of transcription within the long terminal repeat of HIV-1 by tat gene product. Nature 1987; 330: 489
   PubMed Web of Science ®Google Scholar
• Weeks K. M., Ampe C., Schultz S. C., Steitz T. A., Crothers D. M. Fragments of the HIV-1 Tat protein specifically bind TAR RNA. Science 1990; 249: 1281
   PubMed Web of Science ®Google Scholar
• Calnan B. J., Biancalana S., Hudson D., Frankel A. D. Analysis of arginine-rich peptides from the HIV Tat protein reveals unusual features of RNA-protein recognition. Genes Dev. 1991; 5: 201
   PubMed Web of Science ®Google Scholar
• Weeks K. M., Crothers D. M. RNA recognition by Tat-derived peptides: interaction in the major groove. Cell 1991; 66: 577
   PubMed Web of Science ®Google Scholar
• Maderious A., Chen-Kiang S. Pausing and premature termination of human RNA polymerase II during transcription of adenovirus in vivo and in vitro. Proc. Natl. Acad. Sci. U.S.A. 1984; 81: 5931
   PubMed Web of Science ®Google Scholar
• Kessler M., Ben-Asher E., Aloni Y. Elements modulating the block of transcription elongation at the adenovirus 2 attenuation site. J. Biol. Chem. 1989; 264: 9785
   PubMedGoogle Scholar
• Seiberg M., Aloni Y., Levine A. J. The adenovirus type 2 DNA binding protein interacts with the major late promoter attenuated RNA. J. Virol. 1989; 63: 1134
   Google Scholar
• Proudfoot N. J. How RNA polymerase II terminates transcription in higher eukaryotes. Trends Biochem. Sci. 1989; 14: 105
   PubMed Web of Science ®Google Scholar
• Connelly S., Manley J. L. A functional mRNA polyadenylation signal is required for transcription termination by RNA polymerase II. Genes Dev. 1988; 2: 440
   PubMed Web of Science ®Google Scholar
• Neuman de Vegvar H. E., Lund E., Dahlberg J. E. 3′ end formation of U1 snRNA precursors is coupled to transcription from snRNA promoters. Cell 1986; 47: 259
   PubMed Web of Science ®Google Scholar