Investigation of σ70 subunit structure dependence in Escherichia coli RNA polymerase on ionic strength by the molecular dynamics simulation method

被引：0

作者：

Tolstova A.P. ^{[1
]}

Dubrovin E.V. ^{[1
]}

Koroleva O.N. ^{[2
]}

机构：

[1] Department of Physics, Moscow State University, Moscow

[2] Department of Chemistry, Moscow State University, Moscow

来源：

Biophysics | 2015年 / 60卷 / 6期

基金：

俄罗斯基础研究基金会;

关键词：

molecular dynamics; σ[!sup]70[!/sup] subunit of RNA polymerase;

D O I：

10.1134/S0006350915060251

中图分类号：

学科分类号：

摘要：

Modeling of the σ70-subunit of the E. coli RNA polymerase (the small protein in the composition of the RNA-polymerase holoenzyme that is responsible for the specificity of the specificity of the transcription initiation of constitutive genes) was conducted at different salt concentrations. Two variants of the C-terminal domain 4 position in the protein were discovered. In one of them, which was found at low salt concentration in the solution, domain 4 interacted with a 190–210 aa region of the NCR domain that is enriched with negatively charged amino-acid residues. In the second one, the high salt concentration shielded the charged region in the NCR and domain 4 became free, which likely caused the increase of the polymerization rate. The simulation results are not in agreement with any currently existing hypothesis on the positions of the N- and C-terminals during self-inhibition. © 2015, Pleiades Publishing, Inc.

引用

页码：865 / 869

页数：4

共 22 条

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