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Activation of contact-dependent antibacterial tRNase toxins by translation elongation factors.
Jones, Allison M; Garza-Sánchez, Fernando; So, Jaime; Hayes, Christopher S; Low, David A.
Afiliación
  • Jones AM; Department of Molecular, Cellular, and Developmental Biology, University of California, Santa Barbara, CA 93106.
  • Garza-Sánchez F; Department of Molecular, Cellular, and Developmental Biology, University of California, Santa Barbara, CA 93106.
  • So J; Department of Molecular, Cellular, and Developmental Biology, University of California, Santa Barbara, CA 93106.
  • Hayes CS; Department of Molecular, Cellular, and Developmental Biology, University of California, Santa Barbara, CA 93106.
  • Low DA; Biomolecular Science and Engineering Program, University of California, Santa Barbara, CA 93106.
Proc Natl Acad Sci U S A ; 114(10): E1951-E1957, 2017 03 07.
Article en En | MEDLINE | ID: mdl-28223500
Contact-dependent growth inhibition (CDI) is a mechanism by which bacteria exchange toxins via direct cell-to-cell contact. CDI systems are distributed widely among Gram-negative pathogens and are thought to mediate interstrain competition. Here, we describe tsf mutations that alter the coiled-coil domain of elongation factor Ts (EF-Ts) and confer resistance to the CdiA-CTEC869 tRNase toxin from enterohemorrhagic Escherichia coli EC869. Although EF-Ts is required for toxicity in vivo, our results indicate that it is dispensable for tRNase activity in vitro. We find that CdiA-CTEC869 binds to elongation factor Tu (EF-Tu) with high affinity and this interaction is critical for nuclease activity. Moreover, in vitro tRNase activity is GTP-dependent, suggesting that CdiA-CTEC869 only cleaves tRNA in the context of translationally active GTP·EF-Tu·tRNA ternary complexes. We propose that EF-Ts promotes the formation of GTP·EF-Tu·tRNA ternary complexes, thereby accelerating substrate turnover for rapid depletion of target-cell tRNA.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: ARN de Transferencia / Regulación Bacteriana de la Expresión Génica / Factores de Elongación de Péptidos / Factor Tu de Elongación Peptídica / Proteínas de Escherichia coli / Endorribonucleasas / Escherichia coli Enterohemorrágica / Proteínas de la Membrana Tipo de estudio: Prognostic_studies Idioma: En Revista: Proc Natl Acad Sci U S A Año: 2017 Tipo del documento: Article Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: ARN de Transferencia / Regulación Bacteriana de la Expresión Génica / Factores de Elongación de Péptidos / Factor Tu de Elongación Peptídica / Proteínas de Escherichia coli / Endorribonucleasas / Escherichia coli Enterohemorrágica / Proteínas de la Membrana Tipo de estudio: Prognostic_studies Idioma: En Revista: Proc Natl Acad Sci U S A Año: 2017 Tipo del documento: Article Pais de publicación: Estados Unidos