title: Evidence that ribosomal protein S10 itself is a cellular component necessary for transcription antitermination by phage lambda N protein.
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.
authors.forename: A
authors.initials: A
authors.lastname: Das
authors.forename: B
authors.initials: B
authors.lastname: Ghosh
authors.forename: S
authors.initials: S
authors.lastname: Barik
authors.forename: K
authors.initials: K
authors.lastname: Wolska
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics; D010582:Bacteriophage lambda / Q000235:genetics; D003593:Cytoplasm / Q000502:physiology; D004926:Escherichia coli / Q000235:genetics; D009154:Mutation; D010957:Plasmids; D012269:Ribosomal Proteins / Q000502:physiology*; D014157:Transcription Factors / Q000502:physiology*; D014158:Transcription, Genetic; D014764:Viral Proteins / Q000502:physiology*
chemical_list: D001426:Bacterial Proteins; D012269:Ribosomal Proteins; D014157:Transcription Factors; D014764:Viral Proteins