Mycobacterial HelD is a nucleic acids-clearing factor for RNA polymerase

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F20%3A00538228" target="_blank" >RIV/61388971:_____/20:00538228 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/86652036:_____/20:00538228 RIV/68378050:_____/20:00538228 RIV/00216224:14740/20:00118335 RIV/00216208:11320/20:10423322

Výsledek na webu

<a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7749160/" target="_blank" >https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7749160/</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/s41467-020-20158-4" target="_blank" >10.1038/s41467-020-20158-4</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Mycobacterial HelD is a nucleic acids-clearing factor for RNA polymerase

Popis výsledku v původním jazyce

RNA synthesis is central to life, and RNA polymerase (RNAP) depends on accessory factors for recovery from stalled states and adaptation to environmental changes. Here, we investigated the mechanism by which a helicase-like factor HelD recycles RNAP. We report a cryo-EM structure of a complex between the Mycobacterium smegmatis RNAP and HelD. The crescent-shaped HelD simultaneously penetrates deep into two RNAP channels that are responsible for nucleic acids binding and substrate delivery to the active site, thereby locking RNAP in an inactive state. We show that HelD prevents non-specific interactions between RNAP and DNA and dissociates stalled transcription elongation complexes. The liberated RNAP can either stay dormant, sequestered by HelD, or upon HelD release, restart transcription. Our results provide insights into the architecture and regulation of the highly medically-relevant mycobacterial transcription machinery and define HelD as a clearing factor that releases RNAP from nonfunctional complexes with nucleic acids.

Název v anglickém jazyce

Mycobacterial HelD is a nucleic acids-clearing factor for RNA polymerase

Popis výsledku anglicky

RNA synthesis is central to life, and RNA polymerase (RNAP) depends on accessory factors for recovery from stalled states and adaptation to environmental changes. Here, we investigated the mechanism by which a helicase-like factor HelD recycles RNAP. We report a cryo-EM structure of a complex between the Mycobacterium smegmatis RNAP and HelD. The crescent-shaped HelD simultaneously penetrates deep into two RNAP channels that are responsible for nucleic acids binding and substrate delivery to the active site, thereby locking RNAP in an inactive state. We show that HelD prevents non-specific interactions between RNAP and DNA and dissociates stalled transcription elongation complexes. The liberated RNAP can either stay dormant, sequestered by HelD, or upon HelD release, restart transcription. Our results provide insights into the architecture and regulation of the highly medically-relevant mycobacterial transcription machinery and define HelD as a clearing factor that releases RNAP from nonfunctional complexes with nucleic acids.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10606 - Microbiology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2020

Kód důvěrnosti údajů

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

Název periodika

Nature Communications

ISSN

2041-1723

e-ISSN

—

Svazek periodika

11

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

13

Strana od-do

6419

Kód UT WoS článku

000608512400003

EID výsledku v databázi Scopus

2-s2.0-85097759044