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

0538228 - BTÚ 2021 RIV GB eng J - Článek v odborném periodiku
Kouba, T. - Koval, Tomáš - Sudzinová, Petra - Pospíšil, Jiří - Brezovská, Barbora - Hnilicová, Jarmila - Šanderová, Hana - Janoušková, Martina - Šiková, Michaela - Halada, Petr - Sýkora, Michal - Barvík, I. - Nováček, J. - Trundová, Mária - Dušková, Jarmila - Skálová, Tereza - Chon, U. R. - Murakami, K. S. - Dohnálek, Jan - Krásný, Libor
Mycobacterial HelD is a nucleic acids-clearing factor for RNA polymerase.
Nature Communications. Roč. 11, č. 1 (2020), č. článku 6419. E-ISSN 2041-1723
Grant CEP: GA MŠMT(CZ) LM2015043; GA ČR(CZ) GA20-12109S; GA ČR(CZ) GA20-07473S; GA MŠMT(CZ) ED1.1.00/02.0109; GA MŠMT(CZ) EF16_013/0001776
Grant ostatní: OP VVV - ELIBIO(XE) CZ.02.1.01/0.0/0.0/15_003/0000447
Institucionální podpora: RVO:86652036 ; RVO:61388971 ; RVO:68378050
Klíčová slova: DNA-directed RNA Polymerase * Bacterial RNA * Sigma Factors
Obor OECD: Biophysics; Microbiology (MBU-M); Biochemistry and molecular biology (UMG-J)
Impakt faktor: 14.919, rok: 2020
Způsob publikování: Open access
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7749160/

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.
Trvalý link: http://hdl.handle.net/11104/0316062