Solution structure of domain 1.1 of the sigma(A) factor from Bacillus subtilis is preformed for binding to the RNA polymerase core

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F17%3A00477069" target="_blank" >RIV/61388971:_____/17:00477069 - isvavai.cz</a>

Alternative codes found

RIV/00216224:14740/17:00094887 RIV/00216208:11320/17:10370910

Result on the web

<a href="http://dx.doi.org/10.1074/jbc.M117.784074" target="_blank" >http://dx.doi.org/10.1074/jbc.M117.784074</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1074/jbc.M117.784074" target="_blank" >10.1074/jbc.M117.784074</a>

Result language

angličtina

Original language name

Solution structure of domain 1.1 of the sigma(A) factor from Bacillus subtilis is preformed for binding to the RNA polymerase core

Original language description

Bacterial RNA polymerase (RNAP) requires sigma factors to recognize promoter sequences. Domain 1.1 of primary sigma factors (sigma 1.1) prevents their binding to promoter DNA in the absence of RNAP, and when in complex with RNAP, it occupies the DNA-binding channel of RNAP. Currently, two 3D structures of sigma 1.1 are available: from Escherichia coli in complex with RNAP and from T. maritima solved free in solution. However, these two structures significantly differ, and it is unclear whether this difference is due to an altered conformation upon RNAP binding or to differences in intrinsic properties between the proteins from these two distantly related species. Here, we report the solution structure of sigma 1.1 from the Gram-positive bacterium Bacillus subtilis. We found that B. subtilis sigma 1.1 is highly compact because of additional stabilization not present in sigma 1.1 from the other two species and that it is more similar to E. coli sigma 1.1. Moreover, modeling studies suggested that B. subtilis sigma 1.1 requires minimal conformational changes for accommodating RNAP in the DNA channel, whereas T. maritima sigma 1.1 must be rearranged to fit therein. Thus, the mesophilic species B. subtilis and E. coli share the same sigma 1.1 fold, whereas the fold of sigma 1.1 from the thermophile T. maritima is distinctly different. Finally, we describe an intriguing similarity between sigma 1.1 and , an RNAP-associated protein in B. subtilis, bearing implications for the so-far unknown binding site of on RNAP. In conclusion, our results shed light on the conformational changes of sigma 1.1 required for its accommodation within bacterial RNAP.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10606 - Microbiology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2017

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Journal of Biological Chemistry

ISSN

0021-9258

e-ISSN

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Volume of the periodical

292

Issue of the periodical within the volume

28

Country of publishing house

US - UNITED STATES

Number of pages

8

Pages from-to

11610-11617

UT code for WoS article

000405485600002

EID of the result in the Scopus database

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