RNA polymerase recycling by mycobacterial HelD: an alternative, HelD-protected pathway of transcription initiation

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F24%3A00601694" target="_blank" >RIV/61388971:_____/24:00601694 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/86652036:_____/24:00601694 RIV/61388963:_____/24:00601694

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

RNA polymerase recycling by mycobacterial HelD: an alternative, HelD-protected pathway of transcription initiation

Popis výsledku v původním jazyce

Mycobacterial HelD is a transcription factor that binds RNA polymerase (RNAP), dissociates it from nucleic acids and thereby rescues it from stalled transcription complexes. HelD also protects RNAP against the antibiotic rifampicin. The rescued RNAP, however, must disengage from HelD to participate in the next round of transcription. The exact mechanism of this release is unknown. We show that HelD from Mycobacterium smegmatis can form a complex with RNAP associated with the primary nsigma factor SigA and transcription factor RbpA but not CarD. We solved a series of RNAP-SigA-RbpA-HelD structures with or without promoter DNA. These snapshots capture HelD during transcription initiation, describe mechanistic aspects of HelD nrelease 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. Taken together, HelD nmediates an alternative pathway of transcription initiation.nnThis work was supported by the National Institute of Virology and Bacteriology (Program EXCELES, ID Project No. LX22NPO5103) funded by the European Union–Next Generation EU.n

Název v anglickém jazyce

RNA polymerase recycling by mycobacterial HelD: an alternative, HelD-protected pathway of transcription initiation

Popis výsledku anglicky

Mycobacterial HelD is a transcription factor that binds RNA polymerase (RNAP), dissociates it from nucleic acids and thereby rescues it from stalled transcription complexes. HelD also protects RNAP against the antibiotic rifampicin. The rescued RNAP, however, must disengage from HelD to participate in the next round of transcription. The exact mechanism of this release is unknown. We show that HelD from Mycobacterium smegmatis can form a complex with RNAP associated with the primary nsigma factor SigA and transcription factor RbpA but not CarD. We solved a series of RNAP-SigA-RbpA-HelD structures with or without promoter DNA. These snapshots capture HelD during transcription initiation, describe mechanistic aspects of HelD nrelease 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. Taken together, HelD nmediates an alternative pathway of transcription initiation.nnThis work was supported by the National Institute of Virology and Bacteriology (Program EXCELES, ID Project No. LX22NPO5103) funded by the European Union–Next Generation EU.n

Druh

O - Ostatní výsledky

CEP obor

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OECD FORD obor

10606 - Microbiology

Projekt

<a href="/cs/project/LX22NPO5103" target="_blank" >LX22NPO5103: Národní institut virologie a bakteriologie</a><br>

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