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PMID: 2965813 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

NusA protein is necessary and sufficient in vitro for phage lambda N gene product to suppress a rho-independent terminator placed downstream of nutL.

Whalen W, Ghosh B, Das A

Abstract

Transcription antitermination by phage lambda N protein is reproduced in vitro solely with purified components. We have placed a strong rho-independent terminator, lambda tR', in the PL operon about 200 base pairs downstream from the N-recognition site, nutL, and have monitored terminated and run-off transcripts produced by single-round transcription of linear plasmids. In the presence of NusA, one of several host factors implicated in antitermination, N is found to virtually abolish termination at tR'. N is unable to suppress termination if the terminator is preceded by a defective nut site. Thus, during transcription through the nut site, N and NusA can modify RNA polymerase to a termination-resistant form in the absence of any other accessory factor.

MeSH Terms
Bacterial Proteins/physiology Bacteriophage lambda/genetics DNA-Directed RNA Polymerases/metabolism Rho Factor/physiology Terminator Regions, Genetic Transcription Factors/physiology Transcription, Genetic Viral Proteins/physiology
Chemicals
Bacterial Proteins Rho Factor Transcription Factors Viral Proteins DNA-Directed RNA Polymerases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Whalen W
Department of Microbiology, University of Connecticut, Farmington 06032.
Ghosh B
Das A
References (28)
28 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1988-04-00
Pages
2494-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC280023
Subset
IM
Grants
NIGMS NIH HHS · GM28946 · United States
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