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Molecular basis for the unique role of the AAA+ chaperone ClpV in type VI protein secretion

Ring-forming AAA(+) ATPases act in a plethora of cellular processes by remodeling macromolecules. The specificity of individual AAA(+) proteins is achieved by direct or adaptor-mediated association with substrates via distinct recognition domains. We investigated the molecular basis of substrate int...

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Bibliographic Details
Main Authors: Pietrosiuk, Aleksandra (Author) , Lenherr, Esther D. (Author) , Falk, Sebastian (Author) , Bönemann, Gabriele (Author) , Kopp, Jürgen (Author) , Zentgraf, Hanswalter (Author) , Sinning, Irmgard (Author) , Mogk, Axel (Author)
Format: Article (Journal)
Language:English
Published: July 7, 2011
In: The journal of biological chemistry
Year: 2011, Volume: 286, Issue: 34, Pages: 30010-30021
ISSN:1083-351X
DOI:10.1074/jbc.M111.253377
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1074/jbc.M111.253377
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Author Notes:Aleksandra Pietrosiuk, Esther D. Lenherr, Sebastian Falk, Gabriele Bönemann, Jürgen Kopp, Hanswalter Zentgraf, Irmgard Sinning, and Axel Mogk
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Summary:Ring-forming AAA(+) ATPases act in a plethora of cellular processes by remodeling macromolecules. The specificity of individual AAA(+) proteins is achieved by direct or adaptor-mediated association with substrates via distinct recognition domains. We investigated the molecular basis of substrate interaction for Vibrio cholerae ClpV, which disassembles tubular VipA/VipB complexes, an essential step of type VI protein secretion and bacterial virulence. We identified the ClpV recognition site within VipB, showed that productive ClpV-VipB interaction requires the oligomeric state of both proteins, solved the crystal structure of a ClpV N-domain-VipB peptide complex, and verified the interaction surface by mutant analysis. Our results show that the substrate is bound to a hydrophobic groove, which is formed by the addition of a single α-helix to the core N-domain. This helix is absent from homologous N-domains, explaining the unique substrate specificity of ClpV. A limited interaction surface between both proteins accounts for the dramatic increase in binding affinity upon ATP-driven ClpV hexamerization and VipA/VipB tubule assembly by coupling multiple weak interactions. This principle ensures ClpV selectivity toward the VipA/VipB macromolecular complex.
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Physical Description:Online Resource
ISSN:1083-351X
DOI:10.1074/jbc.M111.253377

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