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.

Science 4 May 1990:
Vol. 248. no. 4955, pp. 573 - 578
DOI: 10.1126/science.2185541
Prev | Table of Contents | Next

Articles

Science, Vol 248, Issue 4955, 573-578
Copyright © 1990 by American Association for the Advancement of Science

articles

An RNA polymerase-binding protein that is required for communication between an enhancer and a promoter

DR Herendeen, KP Williams, GA Kassavetis, and EP Geiduschek

Department of Biology, University of California, San Diego, La Jolla 92093.

Although bacteriophage T4 late promoters are selectively recognized by Escherichia coli RNA polymerase bearing a single protein encoded by T4 gene 55 (gp55), efficient transcription at these promoters requires enhancement by the three T4 DNA polymerase accessory proteins, bound to distal "mobile enhancer" sites. Two principles are shown to govern this transcriptional enhancement: (i) Promoter recognition and communication between the enhancer and the promoter require separate phage-coded proteins. Only RNA polymerase that has the T4 gene 33 protein (gp33) bound to it is subject to enhancement by the three DNA replication proteins. (ii) Transcriptional enhancement in this prokaryotic system is promoter-specific. Promoter specificity is generated by a direct competition of phage T4 gp33 and gp55 with the E. coli promoter recognition protein, sigma 70, for binding to the E. coli RNA polymerase core. Thus, polymerase that contains sigma 70 is competent to transcribe T4 early and middle genes, but lacks the ability to be enhanced by the DNA replication proteins, while polymerase that contains gp55 and gp33 is capable of enhancement via gp33, but its activity is restricted to T4 late promoters by gp55.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
The bacteriophage T4 late-transcription coactivator gp33 binds the flap domain of Escherichia coli RNA polymerase.
S. Nechaev, M. Kamali-Moghaddam, E. Andre, J.-P. Leonetti, and E. P. Geiduschek (2004)
PNAS 101, 17365-17370
   Abstract »    Full Text »    PDF »
Snapshot of the Genome of the Pseudo-T-Even Bacteriophage RB49.
C. Desplats, C. Dez, F. Tetart, H. Eleaume, and H. M. Krisch (2002)
J. Bacteriol. 184, 2789-2804
   Abstract »    Full Text »    PDF »
The Carboxyl Terminus of the Bacteriophage T4 DNA Polymerase Contacts Its Sliding Clamp at the Subunit Interface.
S. C. Alley, A. D. Jones, P. Soumillion, and S. J. Benkovic (1999)
J. Biol. Chem. 274, 24485-24489
   Abstract »    Full Text »    PDF »
Abortive Initiation of Transcription at a Hybrid Promoter. AN ANALYSIS OF THE SLIDING CLAMP ACTIVATOR OF BACTERIOPHAGE T4 LATE TRANSCRIPTION, AND A COMPARISON OF THE sigma 70 AND T4 GP55 PROMOTER RECOGNITION PROTEINS.
T.-J. Fu, E. P. Geiduschek, and G. A. Kassavetis (1998)
J. Biol. Chem. 273, 34042-34048
   Abstract »    Full Text »    PDF »
Activation of RNA polymerase II by topologically linked DNA-tracking proteins.
M. Ouhammouch, M. H. Sayre, J. T. Kadonaga, and E. P. Geiduschek (1997)
PNAS 94, 6718-6723
   Abstract »    Full Text »    PDF »
The COOH-terminal Domain of the RNA Polymerase [IMAGE] Subunit in Transcriptional Enhancement and Deactivation at the Bacteriophage T4 Late Promoter.
R. L. Tinker, G. M. Sanders, K. Severinov, G. A. Kassavetis, and E. P. Geiduschek (1995)
J. Biol. Chem. 270, 15899-15907
   Abstract »    Full Text »    PDF »
A transcriptional enhancer whose function imposes a requirement that proteins track along DNA.
D. Herendeen, G. Kassavetis, and E. Geiduschek (1992)
Science 256, 1298-1303
   Abstract »    PDF »
Targeting the E1 replication protein to the papillomavirus origin of replication by complex formation with the E2 transactivator.
I. Mohr, R Clark, S Sun, E. Androphy, P MacPherson, and M. Botchan (1990)
Science 250, 1694-1699
   Abstract »    PDF »


To Advertise     Find Products

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