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.