Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 14 February 1992:
Vol. 255. no. 5046, pp. 838 - 841
DOI: 10.1126/science.1536008
Prev | Table of Contents | Next

Articles

Science, Vol 255, Issue 5046, 838-841
Copyright © 1992 by American Association for the Advancement of Science

articles

Structure of transcription elongation complexes in vivo

M Kainz and J Roberts

Section of Biochemistry, Molecular, and Cell Biology, Cornell University, Ithaca, NY 14853.

The opening of duplex DNA in the elongation phase of transcription by Escherichia coli RNA polymerase in vivo was detected at a regulatory site where a prolonged pause in transcription occurs. Single-stranded DNA in the transcription bubble was identified by its reactivity with potassium permanganate (KMnO4). The elongation structure in vivo was similar to that of transcription complexes made in vitro with some differences. The observed reactivity to KMnO4 of the DNA template strand was consistent with the existence of an RNA-DNA hybrid of about 12 nucleotides.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
The promoter spacer influences transcription initiation via {sigma}70 region 1.1 of Escherichia coli RNA polymerase.
I. G. Hook-Barnard and D. M. Hinton (2009)
PNAS 106, 737-742
   Abstract »    Full Text »    PDF »
Transcription-Dependent Increase in Multiple Classes of Base Substitution Mutations in Escherichia coli.
J. Klapacz and A. S. Bhagwat (2002)
J. Bacteriol. 184, 6866-6872
   Abstract »    Full Text »    PDF »
Inaugural Article: Restructuring of an RNA polymerase holoenzyme elongation complex by lambdoid phage Q proteins.
M. T. Marr, S. A. Datwyler, C. F. Meares, and J. W. Roberts (2001)
PNAS 98, 8972-8978
   Abstract »    Full Text »    PDF »
Recognition of Overlapping Nucleotides by AraC and the Sigma Subunit of RNA Polymerase.
A. Dhiman and R. Schleif (2000)
J. Bacteriol. 182, 5076-5081
   Abstract »    Full Text »
A surface of Escherichia coli sigma 70 required for promoter function and antitermination by phage lambda  Q protein.
D. C. Ko, M. T. Marr, J. Guo, and J. W. Roberts (1998)
Genes & Dev. 12, 3276-3285
   Abstract »    Full Text »
Promoter opening via a DNA fork junction binding activity.
Y. Guo and J. D. Gralla (1998)
PNAS 95, 11655-11660
   Abstract »    Full Text »    PDF »
An Integrated Model of the Transcription Complex in Elongation, Termination, and Editing.
P. H. von Hippel (1998)
Science 281, 660-665
   Abstract »    Full Text »
Information Processing by RNA Polymerase: Recognition of Regulatory Signals during RNA Chain Elongation.
R. A. Mooney, I. Artsimovitch, and R. Landick (1998)
J. Bacteriol. 180, 3265-3275
   Full Text »
Antitermination by Bacteriophage {lambda} Q Protein.
J.W. ROBERTS, W. YARNELL, E. BARTLETT, J. GUO, M. MARR, D.C. KO, H. SUN, and C.W. ROBERTS (1998)
Cold Spring Harb Symp Quant Biol 63, 319-326
   Abstract »    PDF »
Formation and Crystallization of Yeast RNA Polymerase II Elongation Complexes.
A. Gnatt, J. Fu, and R. D. Kornberg (1997)
J. Biol. Chem. 272, 30799-30805
   Abstract »    Full Text »    PDF »
Nuclease Activity of T7 RNA Polymerase and the Heterogeneity of Transcription Elongation Complexes.
S. S. Sastry and B. M. Ross (1997)
J. Biol. Chem. 272, 8644-8652
   Abstract »    Full Text »    PDF »
Model for XPC-independent Transcription-coupled Repair of Pyrimidine Dimers in Humans.
D. Mu and A. Sancar (1997)
J. Biol. Chem. 272, 7570-7573
   Abstract »    Full Text »    PDF »
Nuclease Cleavage of the Upstream Half of the Nontemplate Strand DNA in an Escherichia coli Transcription Elongation Complex Causes Upstream Translocation and Transcriptional Arrest.
D. Wang and R. Landick (1997)
J. Biol. Chem. 272, 5989-5994
   Abstract »    Full Text »    PDF »
Equilibrium and Stopped-flow Kinetic Studies of Interaction between T7 RNA Polymerase and Its Promoters Measured by Protein and 2-Aminopurine Fluorescence Changes.
Y. Jia, A. Kumar, and S. S. Patel (1996)
J. Biol. Chem. 271, 30451-30458
   Abstract »    Full Text »    PDF »
Transcription-induced mutations: Increase in C to T mutations in the nontranscribed strand during transcription in Escherichia coli.
A. Beletskii and A. S. Bhagwat (1996)
PNAS 93, 13919-13924
   Abstract »    Full Text »    PDF »
RNA Polymerase Signals UvrAB Landing Sites.
B. Ahn and L. Grossman (1996)
J. Biol. Chem. 271, 21453-21461
   Abstract »    Full Text »    PDF »
Activator-dependent regulation of transcriptional pausing on nucleosomal templates..
S A Brown, A N Imbalzano, and R E Kingston (1996)
Genes & Dev. 10, 1479-1490
   Abstract »    PDF »
Identification by in Organello Footprinting of Protein Contact Sites and of Single-stranded DNA Sequences in the Regulatory Region of Rat Mitochondrial DNA.
P. Cantatore, L. Daddabbo, F. Fracasso, and M. N. Gadaleta (1995)
J. Biol. Chem. 270, 25020-25027
   Abstract »    Full Text »    PDF »
Molecular matchmakers.
A Sancar and J. Hearst (1993)
Science 259, 1415-1420
   Abstract »    PDF »
Two open complexes and a requirement for Mg2+ to open the lambda PR transcription start site.
W. Suh, W Ross, and M. Record Jr (1993)
Science 259, 358-361
   Abstract »    PDF »
Functional transcription elongation complexes from synthetic RNA-DNA bubble duplexes.
S. Daube and P. von Hippel (1992)
Science 258, 1320-1324
   Abstract »    PDF »
Promoter melting and TFIID complexes on Drosophila genes in vivo..
C Giardina, M Perez-Riba, and J T Lis (1992)
Genes & Dev. 6, 2190-2200
   Abstract »    PDF »
The block to transcriptional elongation within the human c-myc gene is determined in the promoter-proximal region..
A Krumm, T Meulia, M Brunvand, and M Groudine (1992)
Genes & Dev. 6, 2201-2213
   Abstract »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)