PMID:2987961
| Citation |
Das, A , Ghosh, B , Barik, S and Wolska, K (1985) Evidence that ribosomal protein S10 itself is a cellular component necessary for transcription antitermination by phage lambda N protein. Proc. Natl. Acad. Sci. U.S.A. 82:4070-4 |
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| 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. |
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| Keywords |
Bacterial Proteins/genetics; Bacteriophage lambda/genetics; Cytoplasm/physiology; Escherichia coli/genetics; Mutation; Plasmids; Ribosomal Proteins/physiology; Transcription Factors/physiology; Transcription, Genetic; Viral Proteins/physiology |
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