Horwitz R J, Li J, Greenblatt J
Banting and Best Department of Medical Research, Charles H. Best Institute, Toronto, Canada.
Cell. 1987 Nov 20;51(4):631-41. doi: 10.1016/0092-8674(87)90132-2.
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.
噬菌体λ的N基因转录抗终止蛋白在体外被整合到含有大肠杆菌蛋白NusA和NusB的转录延伸复合物中。NusA与延伸中的RNA聚合酶的结合不依赖于序列,且发生在σ70释放之后。将N整合到延伸复合物中需要DNA模板上的一个N利用位点(nut位点)。将NusB整合到复合物中需要NusA、核糖体蛋白S10和nut位点的boxA组分。T1核糖核酸酶从延伸复合物中释放N,但不释放NusB。因此,我们提出一个经N修饰的抗终止延伸复合物包含一个延伸控制颗粒(ECP),其至少含有NusA、NusB、S10、N以及nut位点的一个RNA转录本。