Your browser doesn't support javascript.
loading
Functional plasticity of antibacterial EndoU toxins.
Michalska, Karolina; Quan Nhan, Dinh; Willett, Julia L E; Stols, Lucy M; Eschenfeldt, William H; Jones, Allison M; Nguyen, Josephine Y; Koskiniemi, Sanna; Low, David A; Goulding, Celia W; Joachimiak, Andrzej; Hayes, Christopher S.
Afiliación
  • Michalska K; Midwest Center for Structural Genomics, Argonne National Laboratory, Argonne, IL, USA.
  • Quan Nhan D; Structural Biology Center, Biosciences Division, Argonne National Laboratory, Argonne, IL, USA.
  • Willett JLE; Department of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, CA, USA.
  • Stols LM; Department of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, CA, USA.
  • Eschenfeldt WH; Midwest Center for Structural Genomics, Argonne National Laboratory, Argonne, IL, USA.
  • Jones AM; Midwest Center for Structural Genomics, Argonne National Laboratory, Argonne, IL, USA.
  • Nguyen JY; Department of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, CA, USA.
  • Koskiniemi S; Department of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, CA, USA.
  • Low DA; Department of Cell and Molecular Biology, Uppsala University, Uppsala, Sweden.
  • Goulding CW; Department of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, CA, USA.
  • Joachimiak A; Biomolecular Science and Engineering Program, University of California, Santa Barbara, CA, USA.
  • Hayes CS; Department of Molecular Biology & Biochemistry, University of California, Irvine, CA, USA.
Mol Microbiol ; 109(4): 509-527, 2018 08.
Article en En | MEDLINE | ID: mdl-29923643
Bacteria use several different secretion systems to deliver toxic EndoU ribonucleases into neighboring cells. Here, we present the first structure of a prokaryotic EndoU toxin in complex with its cognate immunity protein. The contact-dependent growth inhibition toxin CdiA-CTSTECO31 from Escherichia coli STEC_O31 adopts the eukaryotic EndoU fold and shares greatest structural homology with the nuclease domain of coronavirus Nsp15. The toxin contains a canonical His-His-Lys catalytic triad in the same arrangement as eukaryotic EndoU domains, but lacks the uridylate-specific ribonuclease activity that characterizes the superfamily. Comparative sequence analysis indicates that bacterial EndoU domains segregate into at least three major clades based on structural variations in the N-terminal subdomain. Representative EndoU nucleases from clades I and II degrade tRNA molecules with little specificity. In contrast, CdiA-CTSTECO31 and other clade III toxins are specific anticodon nucleases that cleave tRNAGlu between nucleotides C37 and m2 A38. These findings suggest that the EndoU fold is a versatile scaffold for the evolution of novel substrate specificities. Such functional plasticity may account for the widespread use of EndoU effectors by diverse inter-bacterial toxin delivery systems.
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: Toxinas Bacterianas / Endorribonucleasas / Escherichia coli / Antibacterianos Idioma: En Revista: Mol Microbiol Asunto de la revista: BIOLOGIA MOLECULAR / MICROBIOLOGIA Año: 2018 Tipo del documento: Article País de afiliación: Estados Unidos 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: Toxinas Bacterianas / Endorribonucleasas / Escherichia coli / Antibacterianos Idioma: En Revista: Mol Microbiol Asunto de la revista: BIOLOGIA MOLECULAR / MICROBIOLOGIA Año: 2018 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido