Your browser doesn't support javascript.
loading
Concerted transformation of a hyper-paused transcription complex and its reinforcing protein.
Zuber, Philipp K; Said, Nelly; Hilal, Tarek; Wang, Bing; Loll, Bernhard; González-Higueras, Jorge; Ramírez-Sarmiento, César A; Belogurov, Georgiy A; Artsimovitch, Irina; Wahl, Markus C; Knauer, Stefan H.
Afiliación
  • Zuber PK; Biochemistry IV-Biophysical Chemistry, Universität Bayreuth, Bayreuth, Germany.
  • Said N; MRC Laboratory of Molecular Biology, Cambridge Biomedical Campus, Cambridge, UK.
  • Hilal T; Institute of Chemistry and Biochemistry, Laboratory of Structural Biochemistry, Freie Universität Berlin, Berlin, Germany.
  • Wang B; Institute of Chemistry and Biochemistry, Laboratory of Structural Biochemistry, Freie Universität Berlin, Berlin, Germany.
  • Loll B; Research Center of Electron Microscopy and Core Facility BioSupraMol, Freie Universität Berlin, Berlin, Germany.
  • González-Higueras J; Department of Microbiology and Center for RNA Biology, The Ohio State University, Columbus, OH, USA.
  • Ramírez-Sarmiento CA; Institute of Chemistry and Biochemistry, Laboratory of Structural Biochemistry, Freie Universität Berlin, Berlin, Germany.
  • Belogurov GA; Institute for Biological and Medical Engineering, Schools of Engineering, Medicine and Biological Sciences, Pontificia Universidad Católica de Chile, Santiago, Chile.
  • Artsimovitch I; ANID, Millennium Science Initiative Program, Millennium Institute for Integrative Biology, Santiago, Chile.
  • Wahl MC; Institute for Biological and Medical Engineering, Schools of Engineering, Medicine and Biological Sciences, Pontificia Universidad Católica de Chile, Santiago, Chile.
  • Knauer SH; ANID, Millennium Science Initiative Program, Millennium Institute for Integrative Biology, Santiago, Chile.
Nat Commun ; 15(1): 3040, 2024 Apr 08.
Article en En | MEDLINE | ID: mdl-38589445
ABSTRACT
RfaH, a paralog of the universally conserved NusG, binds to RNA polymerases (RNAP) and ribosomes to activate expression of virulence genes. In free, autoinhibited RfaH, an α-helical KOW domain sequesters the RNAP-binding site. Upon recruitment to RNAP paused at an ops site, KOW is released and refolds into a ß-barrel, which binds the ribosome. Here, we report structures of ops-paused transcription elongation complexes alone and bound to the autoinhibited and activated RfaH, which reveal swiveled, pre-translocated pause states stabilized by an ops hairpin in the non-template DNA. Autoinhibited RfaH binds and twists the ops hairpin, expanding the RNADNA hybrid to 11 base pairs and triggering the KOW release. Once activated, RfaH hyper-stabilizes the pause, which thus requires anti-backtracking factors for escape. Our results suggest that the entire RfaH cycle is solely determined by the ops and RfaH sequences and provide insights into mechanisms of recruitment and metamorphosis of NusG homologs across all life.
Asunto(s)
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Factores de Transcripción / Proteínas de Escherichia coli Idioma: En Revista: Nat Commun Asunto de la revista: BIOLOGIA / CIENCIA Año: 2024 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Factores de Transcripción / Proteínas de Escherichia coli Idioma: En Revista: Nat Commun Asunto de la revista: BIOLOGIA / CIENCIA Año: 2024 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido