Mycobacterial HelD connects RNA polymerase recycling with transcription initiation

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F24%3A00600304" target="_blank" >RIV/61388971:_____/24:00600304 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/86652036:_____/24:00600304 RIV/61388963:_____/24:00600304 RIV/00216224:90242/24:00139154 RIV/00216208:11310/24:10487061

Výsledek na webu

<a href="https://www.nature.com/articles/s41467-024-52891-5" target="_blank" >https://www.nature.com/articles/s41467-024-52891-5</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/s41467-024-52891-5" target="_blank" >10.1038/s41467-024-52891-5</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Mycobacterial HelD connects RNA polymerase recycling with transcription initiation

Popis výsledku v původním jazyce

Mycobacterial HelD is a transcription factor that recycles stalled RNAP by dissociating it from nucleic acids and, if present, from the antibiotic rifampicin. The rescued RNAP, however, must disengage from HelD to participate in subsequent rounds of transcription. The mechanism of release is unknown. We show that HelD from Mycobacterium smegmatis forms a complex with RNAP associated with the primary sigma factor sigma A and transcription factor RbpA but not CarD. We solve several structures of RNAP-sigma A-RbpA-HelD without and with promoter DNA. These snapshots capture HelD during transcription initiation, describing mechanistic aspects of HelD release from RNAP and its protective effect against rifampicin. Biochemical evidence supports these findings, defines the role of ATP binding and hydrolysis by HelD in the process, and confirms the rifampicin-protective effect of HelD. Collectively, these results show that when HelD is present during transcription initiation, the process is protected from rifampicin until the last possible moment.

Název v anglickém jazyce

Mycobacterial HelD connects RNA polymerase recycling with transcription initiation

Popis výsledku anglicky

Mycobacterial HelD is a transcription factor that recycles stalled RNAP by dissociating it from nucleic acids and, if present, from the antibiotic rifampicin. The rescued RNAP, however, must disengage from HelD to participate in subsequent rounds of transcription. The mechanism of release is unknown. We show that HelD from Mycobacterium smegmatis forms a complex with RNAP associated with the primary sigma factor sigma A and transcription factor RbpA but not CarD. We solve several structures of RNAP-sigma A-RbpA-HelD without and with promoter DNA. These snapshots capture HelD during transcription initiation, describing mechanistic aspects of HelD release from RNAP and its protective effect against rifampicin. Biochemical evidence supports these findings, defines the role of ATP binding and hydrolysis by HelD in the process, and confirms the rifampicin-protective effect of HelD. Collectively, these results show that when HelD is present during transcription initiation, the process is protected from rifampicin until the last possible moment.

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

2024

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

2041-1723

Svazek periodika

15

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

20

Strana od-do

8740

Kód UT WoS článku

001335963600016

EID výsledku v databázi Scopus

2-s2.0-85205949448