作者: Bryce E Nickels , Christine W Roberts , Haitao Sun , Jeffrey W Roberts , Ann Hochschild
DOI: 10.1016/S1097-2765(02)00648-2
关键词: Elongation 、 Transcription (biology) 、 Biology 、 Bacteriophage 、 Molecular biology 、 RNA polymerase 、 Biophysics 、 Protein subunit 、 Cell biology
摘要: Abstract The Q protein of bacteriophage λ is a transcription antiterminator that modifies the elongation properties E. coli RNA polymerase (RNAP). To do this, DNA-bound λQ must first engage paused complex. Here we show this engagement with RNAP involves an interaction between and σ 70 , demonstrating can be target regulation during elongation. Furthermore, provide evidence stabilizes conformation requires disengagement segment from core enzyme. Recent structure-based models posit transition initiation to phase staged displacement core. Our findings support for proposal.