The Core and Holoenzyme Forms of RNA Polymerase from Mycobacterium smegmatis
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F19%3A00504290" target="_blank" >RIV/61388971:_____/19:00504290 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11310/19:10391988 RIV/00216208:11320/19:10391988
Result on the web
<a href="https://jb.asm.org/content/201/4/e00583-18" target="_blank" >https://jb.asm.org/content/201/4/e00583-18</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1128/JB.00583-18" target="_blank" >10.1128/JB.00583-18</a>
Alternative languages
Result language
angličtina
Original language name
The Core and Holoenzyme Forms of RNA Polymerase from Mycobacterium smegmatis
Original language description
Bacterial RNA polymerase (RNAP) is essential for gene expression and as such is a valid drug target. Hence, it is imperative to know its structure and dynamics. Here, we present two as-yet-unreported forms of Mycobacterium smegmatis RNAP: core and holoenzyme containing sigma(A) but no other factors. Each form was detected by cryo-electron microscopy in two major conformations. Comparisons of these structures with known structures of other RNAPs reveal a high degree of conformational flexibility of the mycobacterial enzyme and confirm that region 1.1 of sigma(A) is directed into the primary channel of RNAP. Taken together, we describe the conformational changes of unrestrained mycobacterial RNAP. nIMPORTANCE We describe here three-dimensional structures of core and holoenzyme forms of mycobacterial RNA polymerase (RNAP) solved by cryo-electron microscopy. These structures fill the thus-far-empty spots in the gallery of the pivotal forms of mycobacterial RNAP and illuminate the extent of conformational dynamics of this enzyme. The presented findings may facilitate future designs of antimycobacterial drugs targeting RNAP.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - 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
Result continuities
Project
—
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2019
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Bacteriology
ISSN
0021-9193
e-ISSN
—
Volume of the periodical
201
Issue of the periodical within the volume
4
Country of publishing house
US - UNITED STATES
Number of pages
12
Pages from-to
e00583
UT code for WoS article
000456875400007
EID of the result in the Scopus database
2-s2.0-85060632900