The Core and Holoenzyme Forms of RNA Polymerase from Mycobacterium smegmatis

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/00216208:11310/19:10391988 RIV/00216208:11320/19:10391988

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

The Core and Holoenzyme Forms of RNA Polymerase from Mycobacterium smegmatis

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

The Core and Holoenzyme Forms of RNA Polymerase from Mycobacterium smegmatis

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10606 - Microbiology

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2019

Kód důvěrnosti údajů

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

Název periodika

Journal of Bacteriology

ISSN

0021-9193

e-ISSN

—

Svazek periodika

201

Číslo periodika v rámci svazku

4

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

12

Strana od-do

e00583

Kód UT WoS článku

000456875400007

EID výsledku v databázi Scopus

2-s2.0-85060632900