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Formation of a Secretion-Competent Protein Complex by a Dynamic Wrap-around Binding Mechanism
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
Vise andre og tillknytning
2018 (engelsk)Inngår i: Journal of Molecular Biology, ISSN 0022-2836, E-ISSN 1089-8638, Vol. 430, nr 18, Part B, s. 3157-3169Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Bacterial virulence is typically initiated by translocation of effector or toxic proteins across host cell membranes. A class of gram-negative pathogenic bacteria including Yersinia pseudotuberculosis and Yersinia pestis accomplishes this objective with a protein assembly called the type III secretion system. Yersinia effector proteins (Yop) are presented to the translocation apparatus through formation of specific complexes with their cognate chaperones (Syc). In the complexes where the structure is available, the Yops are extended and wrap around their cognate chaperone. This structural architecture enables secretion of the Yop from the bacterium in early stages of translocation. It has been shown previously that the chaperone-binding domain of YopE is disordered in its isolation but becomes substantially more ordered in its wrap-around complex with its chaperone SycE. Here, by means of NMR spectroscopy, small-angle X-ray scattering and molecular modeling, we demonstrate that while the free chaperone-binding domain of YopH (YopHCBD) adopts a fully ordered and globular fold, it populates an elongated, wrap-around conformation when it engages in a specific complex with its chaperone SycH2. Hence, in contrast to YopE that is unstructured in its free state, YopH transits from a globular free state to an elongated chaperone-bound state. We demonstrate that a sparsely populated YopHCBD state has an elevated affinity for SycH2 and represents an intermediate in the formation of the protein complex. Our results suggest that Yersinia has evolved a binding mechanism where SycH2 passively stimulates an elongated YopH conformation that is presented to the type III secretion system in a secretion-competent conformation.

sted, utgiver, år, opplag, sider
Elsevier, 2018. Vol. 430, nr 18, Part B, s. 3157-3169
Emneord [en]
NMR spectroscopy, protein complex, binding mechanism
HSV kategori
Identifikatorer
URN: urn:nbn:se:umu:diva-151495DOI: 10.1016/j.jmb.2018.07.014ISI: 000444668100010OAI: oai:DiVA.org:umu-151495DiVA, id: diva2:1245331
Forskningsfinansiär
Swedish Research Council, 2013-5954Knut and Alice Wallenberg FoundationCarl Tryggers foundation , CTS 15:210The Kempe FoundationsTilgjengelig fra: 2018-09-05 Laget: 2018-09-05 Sist oppdatert: 2018-10-04bibliografisk kontrollert

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Gupta, Arun A.Jonna, Venkateswara RaoHofer, AndersWolf-Watz, Magnus

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