Cisneros B, Vaca S, Sosa L, Montañez C
Departamento de Genética y Biología Molecular, Centro de Investigación y de Estudios Avanzados del I.P.N., México, D.F., Mexico.
Rev Latinoam Microbiol. 1994 Jan-Mar;36(1):9-15.
The N protein of bacteriophage lambda modifies Escherichia coli RNA polymerase in such a way that it transcribes through termination signals, in a process called antitermination. In general N-mutants are not able to perform transcription antitermination. In this paper we report the suppression of N7 and Nmar3 mutations by Escherichia coli ron-lon strain. The lon mutation causes the N protein half-life to raise, suggesting that excess of N7 fragment or Nmar3 protein overcome the defect in antitermination. Under these conditions the lambda N-phages produced a titer similar to lambda wild type, although the plaques were smaller. These observations highlight the relevance of N half life in the regulation of transcription antitermination.
噬菌体λ的N蛋白以一种在称为抗终止的过程中通过终止信号进行转录的方式修饰大肠杆菌RNA聚合酶。一般来说,N突变体无法进行转录抗终止。在本文中,我们报道了大肠杆菌ron-lon菌株对N7和Nmar3突变的抑制作用。lon突变导致N蛋白半衰期延长,这表明过量的N7片段或Nmar3蛋白克服了抗终止缺陷。在这些条件下,λ N噬菌体产生的滴度与λ野生型相似,尽管噬菌斑较小。这些观察结果突出了N半衰期在转录抗终止调控中的相关性。