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TitleCryo-EM structure of transcription termination factor Rho from Mycobacterium tuberculosis reveals bicyclomycin resistance mechanism.
Journal, issue, pagesCommun Biol, Vol. 5, Issue 1, Page 120, Year 2022
Publish dateFeb 9, 2022
AuthorsEmmanuel Saridakis / Rishi Vishwakarma / Josephine Lai-Kee-Him / Kevin Martin / Isabelle Simon / Martin Cohen-Gonsaud / Franck Coste / Patrick Bron / Emmanuel Margeat / Marc Boudvillain /
PubMed AbstractThe bacterial Rho factor is a ring-shaped motor triggering genome-wide transcription termination and R-loop dissociation. Rho is essential in many species, including in Mycobacterium tuberculosis ...The bacterial Rho factor is a ring-shaped motor triggering genome-wide transcription termination and R-loop dissociation. Rho is essential in many species, including in Mycobacterium tuberculosis where rho gene inactivation leads to rapid death. Yet, the M. tuberculosis Rho [Rho] factor displays poor NTPase and helicase activities, and resistance to the natural Rho inhibitor bicyclomycin [BCM] that remain unexplained. To address these issues, we solved the cryo-EM structure of Rho at 3.3 Å resolution. The Rho hexamer is poised into a pre-catalytic, open-ring state wherein specific contacts stabilize ATP in intersubunit ATPase pockets, thereby explaining the cofactor preference of Rho. We reveal a leucine-to-methionine substitution that creates a steric bulk in BCM binding cavities near the positions of ATP γ-phosphates, and confers resistance to BCM at the expense of motor efficiency. Our work contributes to explain the unusual features of Rho and provides a framework for future antibiotic development.
External linksCommun Biol / PubMed:35140348 / PubMed Central
MethodsEM (single particle)
Resolution3.32 Å
Structure data

12701

7oqh

EMDB-12701: CryoEM structure of the transcription termination factor Rho from Mycrobacterium Tuberculosis
PDB-7oqh: CryoEM structure of the transcription termination factor Rho from Mycobacterium tuberculosis
Method: EM (single particle) / Resolution: 3.32 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

ChemComp-MG:
Unknown entry

Source
  • mycobacterium tuberculosis (bacteria)
KeywordsTRANSCRIPTION / transcription termination factor / RNA helicase / ATP-dependent / molecular motor

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