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Proteolytic processing induces a conformational switch required for antibacterial toxin delivery.
Bartelli, Nicholas L; Passanisi, Victor J; Michalska, Karolina; Song, Kiho; Nhan, Dinh Q; Zhou, Hongjun; Cuthbert, Bonnie J; Stols, Lucy M; Eschenfeldt, William H; Wilson, Nicholas G; Basra, Jesse S; Cortes, Ricardo; Noorsher, Zainab; Gabraiel, Youssef; Poonen-Honig, Isaac; Seacord, Elizabeth C; Goulding, Celia W; Low, David A; Joachimiak, Andrzej; Dahlquist, Frederick W; Hayes, Christopher S.
Afiliación
  • Bartelli NL; Department of Chemistry and Biochemistry, University of California, Santa Barbara, CA, USA.
  • Passanisi VJ; Department of Chemistry and Biochemistry, University of California, Santa Barbara, CA, USA.
  • Michalska K; Midwest Center for Structural Genomics, Argonne National Laboratory, Lemont, IL, USA.
  • Song K; Center for Structural Genomics of Infectious Diseases, University of Chicago, Chicago, IL, USA.
  • Nhan DQ; Structural Biology Center, X-ray Science Division, Argonne National Laboratory, Lemont, IL, USA.
  • Zhou H; Biomolecular Science and Engineering Program, University of California, Santa Barbara, CA, USA.
  • Cuthbert BJ; Department of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, CA, USA.
  • Stols LM; Department of Chemistry and Biochemistry, University of California, Santa Barbara, CA, USA.
  • Eschenfeldt WH; Department of Molecular Biology & Biochemistry, University of California, Irvine, CA, USA.
  • Wilson NG; Midwest Center for Structural Genomics, Argonne National Laboratory, Lemont, IL, USA.
  • Basra JS; Midwest Center for Structural Genomics, Argonne National Laboratory, Lemont, IL, USA.
  • Cortes R; Department of Chemistry and Biochemistry, University of California, Santa Barbara, CA, USA.
  • Noorsher Z; Department of Chemistry and Biochemistry, University of California, Santa Barbara, CA, USA.
  • Gabraiel Y; Department of Chemistry and Biochemistry, University of California, Santa Barbara, CA, USA.
  • Poonen-Honig I; Department of Chemistry and Biochemistry, University of California, Santa Barbara, CA, USA.
  • Seacord EC; Department of Chemistry and Biochemistry, University of California, Santa Barbara, CA, USA.
  • Goulding CW; Department of Chemistry and Biochemistry, University of California, Santa Barbara, CA, USA.
  • Low DA; Department of Chemistry and Biochemistry, University of California, Santa Barbara, CA, USA.
  • Joachimiak A; Department of Molecular Biology & Biochemistry, University of California, Irvine, CA, USA.
  • Dahlquist FW; Pharmaceutical Sciences, University of California, Irvine, CA, USA.
  • Hayes CS; Biomolecular Science and Engineering Program, University of California, Santa Barbara, CA, USA.
Nat Commun ; 13(1): 5078, 2022 08 29.
Article en En | MEDLINE | ID: mdl-36038560
ABSTRACT
Many Gram-negative bacteria use CdiA effector proteins to inhibit the growth of neighboring competitors. CdiA transfers its toxic CdiA-CT region into the periplasm of target cells, where it is released through proteolytic cleavage. The N-terminal cytoplasm-entry domain of the CdiA-CT then mediates translocation across the inner membrane to deliver the C-terminal toxin domain into the cytosol. Here, we show that proteolysis not only liberates the CdiA-CT for delivery, but is also required to activate the entry domain for membrane translocation. Translocation function depends on precise cleavage after a conserved VENN peptide sequence, and the processed ∆VENN entry domain exhibits distinct biophysical and thermodynamic properties. By contrast, imprecisely processed CdiA-CT fragments do not undergo this transition and fail to translocate to the cytoplasm. These findings suggest that CdiA-CT processing induces a critical structural switch that converts the entry domain into a membrane-translocation competent conformation.
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Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Proteínas de Escherichia coli Idioma: En Revista: Nat Commun Asunto de la revista: BIOLOGIA / CIENCIA Año: 2022 Tipo del documento: Article País de afiliación: Estados Unidos
Texto completo
Imprimir
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PubMed Links
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Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Proteínas de Escherichia coli Idioma: En Revista: Nat Commun Asunto de la revista: BIOLOGIA / CIENCIA Año: 2022 Tipo del documento: Article País de afiliación: Estados Unidos