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dc.contributor.authorChaudhury, Sukanya
dc.contributor.authorde Azevedo Souza, Clarice
dc.contributor.authorPlano, Gregory V.
dc.contributor.authorDe Guzman, Roberto N.
dc.date.accessioned2017-03-27T21:01:41Z
dc.date.available2017-03-27T21:01:41Z
dc.date.issued2015-08-07
dc.identifier.citationChaudhury, Sukanya, Clarice De Azevedo Souza, Gregory V. Plano, and Roberto N. De Guzman. "The LcrG Tip Chaperone Protein of the Yersinia Pestis Type III Secretion System Is Partially Folded." Journal of Molecular Biology 427.19 (2015): 3096-109.en_US
dc.identifier.urihttp://hdl.handle.net/1808/23491
dc.description.abstractThe type III secretion system (T3SS) is essential in the pathogenesis of Yersinia pestis, the causative agent of plague. A small protein, LcrG, functions as a chaperone to the tip protein LcrV, and the LcrG-LcrV interaction is important in regulating protein secretion through the T3SS. The atomic structure of the LcrG family is currently unknown. However, because of its predicted helical propensity, many have suggested that the LcrG family forms a coiled-coil structure. Here, we show by NMR and CD spectroscopy that LcrG lacks a tertiary structure and it consists of three partially folded alpha helices spanning residues 7-38, 41-46, and 58-73. NMR titrations of LcrG with LcrV show that the entire length of a truncated LcrG (residues 7-73) is involved in binding to LcrV. However, there is regional variation in how LcrG binds to LcrV. The C-terminal region of a truncated LcrG (residues 52-73) shows tight-binding interaction with LcrV while the N-terminal region (residues 7-51) shows weaker interaction with LcrV. This suggests there are at least two binding events when LcrG binds to LcrV. Biological assays and mutagenesis indicate that the C-terminal region of LcrG (residues 52-73) is important in blocking protein secretion through the T3SS. Our results reveal structural and mechanistic insights into the atomic conformation of LcrG and how it binds to LcrV.en_US
dc.publisherElsevieren_US
dc.rightsThis is an open access article under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License 3.0 (CC BY-NC-ND 3.0 US), which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.en_US
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/
dc.subjectLcrGen_US
dc.subjectYersinia pestisen_US
dc.subjectT3SSen_US
dc.subjectNMRen_US
dc.subjectTip chaperoneen_US
dc.titleThe LcrG tip chaperone protein of the Yersinia pestis type III secretion system is partially foldeden_US
dc.typeArticleen_US
kusw.kuauthorDe Guzman, Roberto N.
kusw.kudepartmentMolecular Biosciencesen_US
dc.identifier.doi10.1016/j.jmb.2015.07.024en_US
kusw.oaversionScholarly/refereed, author accepted manuscripten_US
kusw.oapolicyThis item meets KU Open Access policy criteria.en_US
dc.rights.accessrightsopenAccess


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This is an open access article under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License 3.0 (CC BY-NC-ND 3.0 US), which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.
Except where otherwise noted, this item's license is described as: This is an open access article under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License 3.0 (CC BY-NC-ND 3.0 US), which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.