PMID: 7027254Jul 1, 1981Paper

Synthetic sites for transcription termination and a functional comparison with tryptophan operon termination sites in vitro

Proceedings of the National Academy of Sciences of the United States of America
G E ChristieT Platt

Abstract

Termination of transcription by Escherichia coli RNA polymerase in vitro appears to depend primarily on two structural features of the termination site--a G+C-rich region of dyad symmetry and a series of terminal uridine residues in the transcript. To determine whether these two features are sufficient to specify rho-independent termination in vitro, we have introduced new sequences within a tryptophan (trp) operon structural gene to create two sites with these characteristics. Transcription with wild-type RNA polymerase in vitro demonstrates that discrete termination occurs at one of these new sites, although at a low level. Use of the mutant RNA polymerase rpo203, which is more sensitive to certain weak terminators than is the wild-type enzyme, increases termination at both sites. We have compared the activity of our synthetic terminators with those of several termination sites in the E. coli trp operon. Under normal conditions of transcription in vitro, termination becomes more efficient with an increase in the length of the stem in the RNA hairpin or an increase in the number of consecutive uridine residues. Transcription with the rpo203 polymerase and with ribonucleotide analogs gives changes consistent with these general ...Continue Reading

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Citations

Jul 1, 1987·Molecular & General Genetics : MGG·H KouharaK Matsubara
Jan 1, 1985·Molecular & General Genetics : MGG·M Tanaka, S Hiraga
Jul 26, 1996·Molecular & General Genetics : MGG·T IwakiF Imamoto
Jan 1, 1986·Progress in Biophysics and Molecular Biology·A Wada, A Suyama
Oct 1, 1982·Proceedings of the National Academy of Sciences of the United States of America·L F LauR Wu
Feb 1, 1982·Proceedings of the National Academy of Sciences of the United States of America·P J Farnham, T Platt
Jan 1, 1983·Proceedings of the National Academy of Sciences of the United States of America·C L TurnboughJ P Donahue
Mar 1, 1983·Proceedings of the National Academy of Sciences of the United States of America·M Navre, H K Schachman
Jul 1, 1985·Proceedings of the National Academy of Sciences of the United States of America·H L Levin, H K Schachman
Dec 1, 1986·Proceedings of the National Academy of Sciences of the United States of America·R P LegockiA A Szalay
Oct 1, 1988·Proceedings of the National Academy of Sciences of the United States of America·K L RolandC L Turnbough
Jun 1, 1989·Proceedings of the National Academy of Sciences of the United States of America·A P VasserotM L Birnstiel
Mar 15, 1991·Proceedings of the National Academy of Sciences of the United States of America·P H von Hippel, T D Yager
Mar 11, 1992·Proceedings of the National Academy of Sciences of the United States of America·C H Jones, C P Moran
Sep 25, 1982·Nucleic Acids Research·H Horowitz, T Platt
Jan 26, 1987·Nucleic Acids Research·C A Gilchrist, D T Denhardt
Mar 11, 1987·Nucleic Acids Research·R P LawtherG W Hatfield
May 11, 1988·Nucleic Acids Research·R LloubèsC Lazdunski
Jul 1, 1987·European Journal of Biochemistry·G MichaelsF E Nargang
Jul 1, 1989·European Journal of Biochemistry·J A KnottA Weston
Feb 2, 2002·Applied and Environmental Microbiology·L G Bermúdez-HumaránYves Le Loir
Dec 9, 2003·Applied and Environmental Microbiology·Yakhya DieyeJean-Christophe Piard
Sep 4, 2004·Applied and Environmental Microbiology·D Llull, I Poquet
Jun 22, 2001·Journal of Bacteriology·Y DieyeJ C Piard
Mar 20, 2010·Canadian Journal of Microbiology·Miguel Martínez-TrujilloCecilia Montañez

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