JBC Avanti Polar Lipids

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Mote Jr., J.
Right arrow Articles by Reines, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mote Jr., J.
Right arrow Articles by Reines, D.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J Biol Chem, Vol. 273, Issue 27, 16843-16852, July 3, 1998

Recognition of a Human Arrest Site Is Conserved between RNA Polymerase II and Prokaryotic RNA Polymerases

John Mote Jr. and Daniel Reines

From the Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322

DNA sequences that arrest transcription by either eukaryotic RNA polymerase II or Escherichia coli RNA polymerase have been identified previously. Elongation factors SII and GreB are RNA polymerase-binding proteins that enable readthrough of arrest sites by these enzymes, respectively. This functional similarity has led to general models of elongation applicable to both eukaryotic and prokaryotic enzymes. Here we have transcribed with phage and bacterial RNA polymerases, a human DNA sequence previously defined as an arrest site for RNA polymerase II. The phage and bacterial enzymes both respond efficiently to the arrest signal in vitro at limiting levels of nucleoside triphosphates. The E. coli polymerase remains in a template-engaged complex for many hours, can be isolated, and is potentially active. The enzyme displays a relatively slow first-order loss of elongation competence as it dwells at the arrest site. Bacterial RNA polymerase arrested at the human site is reactivated by GreB in the same way that RNA polymerase II arrested at this site is stimulated by SII. Very efficient readthrough can be achieved by phage, bacterial, and eukaryotic RNA polymerases in the absence of elongation factors if 5-Br-UTP is substituted for UTP. These findings provide additional and direct evidence for functional similarity between prokaryotic and eukaryotic transcription elongation and readthrough mechanisms.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Biophys. JHome page
M. Voliotis, N. Cohen, C. Molina-Paris, and T. B. Liverpool
Fluctuations, Pauses, and Backtracking in DNA Transcription
Biophys. J., January 15, 2008; 94(2): 334 - 348.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
H.-J. Kim, S.-H. Jeong, J.-H. Heo, S.-J. Jeong, S.-T. Kim, H.-D. Youn, J.-W. Han, H.-W. Lee, and E.-J. Cho
mRNA Capping Enzyme Activity Is Coupled to an Early Transcription Elongation
Mol. Cell. Biol., July 15, 2004; 24(14): 6184 - 6193.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
W. Walter, M. L. Kireeva, V. M. Studitsky, and M. Kashlev
Bacterial Polymerase and Yeast Polymerase II Use Similar Mechanisms for Transcription through Nucleosomes
J. Biol. Chem., September 19, 2003; 278(38): 36148 - 36156.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
L. A. Guarino, W. Dong, and J. Jin
In Vitro Activity of the Baculovirus Late Expression Factor LEF-5
J. Virol., November 13, 2002; 76(24): 12663 - 12675.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
D. Kulish and K. Struhl
TFIIS Enhances Transcriptional Elongation through an Artificial Arrest Site In Vivo
Mol. Cell. Biol., July 1, 2001; 21(13): 4162 - 4168.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
I. Artsimovitch, V. Svetlov, L. Anthony, R. R. Burgess, and R. Landick
RNA Polymerases from Bacillus subtilis and Escherichia coli Differ in Recognition of Regulatory Signals In Vitro
J. Bacteriol., November 1, 2000; 182(21): 6027 - 6035.
[Abstract] [Full Text]

Home page
 Proc. Natl. Acad. Sci. USAHome page
I. Artsimovitch and R. Landick
Pausing by bacterial RNA polymerase is mediated by mechanistically distinct classes of signals
PNAS, June 20, 2000; 97(13): 7090 - 7095.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. L. Kireeva, N. Komissarova, D. S. Waugh, and M. Kashlev
The 8-Nucleotide-long RNA:DNA Hybrid Is a Primary Stability Determinant of the RNA Polymerase II Elongation Complex
J. Biol. Chem., February 25, 2000; 275(9): 6530 - 6536.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. G. Brieba, V. Gopal, and R. Sousa
Scanning Mutagenesis Reveals Roles for Helix N of the Bacteriophage T7 RNA Polymerase Thumb Subdomain in Transcription Complex Stability, Pausing, and Termination
J. Biol. Chem., March 23, 2001; 276(13): 10306 - 10313.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1998 by the American Society for Biochemistry and Molecular Biology.