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PMID: 2987961 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Evidence that ribosomal protein S10 itself is a cellular component necessary for transcription antitermination by phage lambda N protein.

Das A, Ghosh B, Barik S, Wolska K

Abstract

Bacteriophage lambda N gene product acts to modify host RNA polymerase allowing the formation of a termination-resistant transcription apparatus. Previous studies have demonstrated that the nusE71 mutation that has altered the ribosomal protein S10 prevents N action in vivo. Using a coupled transcription-translation system, we demonstrate here that purified S10 protein as well as the 30S ribosomal subunit is sufficient to restore N activity in the nusE mutant extract, allowing antitermination of Rho-dependent and Rho-independent terminators. This provides direct biochemical evidence that the S10 protein itself is one of the cellular components necessary for the formation of an antitermination apparatus.

MeSH Terms
Bacterial Proteins/genetics Bacteriophage lambda/genetics Cytoplasm/physiology Escherichia coli/genetics Mutation Plasmids Ribosomal Proteins/physiology Transcription Factors/physiology Transcription, Genetic Viral Proteins/physiology
Chemicals
Bacterial Proteins Ribosomal Proteins Transcription Factors Viral Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Das A
Ghosh B
Barik S
Wolska K
References (32)
32 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
1985-06-00
Pages
4070-4
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC397936
Subset
IM
Grants
NIGMS NIH HHS · GM28946 · United States
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