The σ70 Subunit of RNA Polymerase Is Contacted by the λQ Antiterminator during Early Elongation

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: ElongationTranscription (biology)BiologyBacteriophageMolecular biologyRNA polymeraseBiophysicsProtein subunitCell 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.

参考文章(32)
Hong Tang, Younggyu Kim, Konstantine Severinov, Alex Goldfarb, Richard H. Ebright, Escherichia coli RNA polymerase holoenzyme: rapid reconstitution from recombinant alpha, beta, beta', and sigma subunits. Methods in Enzymology. ,vol. 273, pp. 130- 134 ,(1996) , 10.1016/S0076-6879(96)73012-4
Jeffrey H Miller, Experiments in molecular genetics ,(1972)
M Lonetto, M Gribskov, C A Gross, The sigma 70 family: sequence conservation and evolutionary relationships. Journal of Bacteriology. ,vol. 174, pp. 3843- 3849 ,(1992) , 10.1128/JB.174.12.3843-3849.1992
S. L. Dove, F. W. Huang, A. Hochschild, Mechanism for a transcriptional activator that works at the isomerization step Proceedings of the National Academy of Sciences of the United States of America. ,vol. 97, pp. 13215- 13220 ,(2000) , 10.1073/PNAS.97.24.13215