title: [Investigation of the Dependence of Escherichia coli RNA Polymerase σ70-Subunit Structure on Ionic Strength by Molecular Dynamics Simulation Method].
abstract: The σ70-subunit of E. coli RNA polymerase (a small protein, being a part of RNA holoenzyme, and responsible for initiation of transcription of constitutive genes) is modeled at different ionic strengths. Two variants of the location of C-end domain 4 are obtained. At low ionic strength domain 4 interacts with the region of high negative charge 190-210 AK within NCR domain. At high ionic strength this region was screened and domain 4 was free and set away from domain NCR. We suppose that this leads to the increase in polymerization rate. Simulation data do not confirm any hypothesis about a self-inhibition mechanism.
authors: A P
authors: AP
authors: Tolstova
authors: E V
authors: EV
authors: Dubrovin
authors: O N
authors: ON
authors: Koroleva
mesh_terms: D055592:Biophysical Phenomena; D012321:DNA-Directed RNA Polymerases / Q000737:chemistry*; D004926:Escherichia coli / Q000737:chemistry* / Q000235:genetics; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D009994:Osmolar Concentration; D011487:Protein Conformation / Q000187:drug effects; D021122:Protein Subunits / Q000737:chemistry; D012492:Salts / Q000737:chemistry; D012808:Sigma Factor / Q000737:chemistry*; D014158:Transcription, Genetic
chemical_list: D021122:Protein Subunits; D012492:Salts; D012808:Sigma Factor; C081775:RNA polymerase sigma 70; D012321:DNA-Directed RNA Polymerases