Altering the interaction between σ 70 and RNA polymerase generates complexes with distinct transcription-elongation properties
Author(s) -
Yvonne Berghöfer-Hochheimer,
Chi Zen Lu,
Carol A. Gross
Publication year - 2005
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.0408973102
Subject(s) - polymerase , rna polymerase ii , rna polymerase , rna polymerase ii holoenzyme , transcription factor ii d , termination factor , rna dependent rna polymerase , rna polymerase i , transcription (linguistics) , small nuclear rna , rna , biology , microbiology and biotechnology , biophysics , chemistry , biochemistry , enzyme , gene expression , gene , promoter , linguistics , philosophy
We compare the elongation behavior of native Escherichia coli RNA polymerase holoenzyme assembled in vivo, holoenzyme reconstituted from sigma70 and RNA polymerase in vitro, and holoenzyme with a specific alteration in the interface between sigma70 and RNA polymerase. Elongating RNA polymerase from each holoenzyme has distinguishable properties, some of which cannot be explained by differential retention or rebinding of sigma70 during elongation, or by differential presence of elongation factors. We suggest that interactions between RNA polymerase and sigma70 may influence the ensemble of conformational states adopted by RNA polymerase during initiation. These states, in turn, may affect the conformational states adopted by the elongating enzyme, thereby physically and functionally imprinting RNA polymerase.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom