Conserved structural mechanisms for autoinhibition in IpaH ubiquitin ligases

Yang Chieh Chou, Alexander F.A. Keszei, John R. Rohde, Mike Tyers, Frank Sicheri

Producción científica: Contribución a una revistaArtículorevisión exhaustiva

39 Citas (Scopus)

Resumen

The IpaH family of novel E3 ligase (NEL) enzymes occur in a variety of pathogenic and commensal bacteria that interact with eukaryotic hosts. We demonstrate that the leucine-rich repeat (LRR) substrate recognition domains of different IpaH enzymes autoinhibit the enzymatic activity of the adjacent catalytic novel E3 ligase domain by two distinct but conserved structural mechanisms. Autoinhibition is required for the in vivo biological activity of two IpaH enzymes in a eukaryotic model system. Autoinhibition was retro-engineered into a constitutively active IpaH enzyme from Yersinia pestis by introduction of single site substitutions, thereby demonstrating the conservation of autoregulatory infrastructure across the IpaH enzyme family.

Idioma originalEnglish
Páginas (desde-hasta)268-275
Número de páginas8
PublicaciónJournal of Biological Chemistry
Volumen287
N.º1
DOI
EstadoPublished - ene. 2 2012

ASJC Scopus Subject Areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

PubMed: MeSH publication types

  • Journal Article
  • Research Support, Non-U.S. Gov't

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