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Evidence That Ribosomal Protein S10 Itself is a Cellular Component Necessary for Transcription Antitermination by Phage λ N Protein

Bacteriophage λ 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...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1985-06, Vol.82 (12), p.4070-4074
Main Authors: Das, Asis, Ghosh, Balaram, Barik, Sailen, Wolska, Krystyna
Format: Article
Language:English
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Summary:Bacteriophage λ 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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.82.12.4070