An elongation control particle containing the N gene transcriptional antitermination protein of bacteriophage lambda.
The N gene transcriptional antitermination protein of bacteriophage lambda is incorporated in vitro into transcriptional elongation complexes containing the E. coli proteins NusA and NusB. The binding of NusA to elongating RNA polymerase is sequence-independent and follows the release of sigma 70. Incorporation of N into the elongation complex requires an N utilization site (nut site) on the DNA template. Incorporation of NusB into the complex requires NusA, ribosomal protein S10, and the boxA component of the nut site. T1 RNAase releases N, but not NusB, from the elongation complex. We therefore propose that an N-modified termination-resistant elongation complex includes an elongation control particle (ECP) containing at least NusA, NusB, S10, N, and an RNA transcript of the nut site.
D001426:Bacterial Proteins / Q000378:metabolism*; D010582:Bacteriophage lambda / Q000235:genetics*; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D008957:Models, Genetic; D012329:RNA, Bacterial / Q000378:metabolism; D013728:Terminator Regions, Genetic; D014158:Transcription, Genetic; D014764:Viral Proteins / Q000502:physiology*
D001426:Bacterial Proteins; D012329:RNA, Bacterial; D014764:Viral Proteins; D012321:DNA-Directed RNA Polymerases