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Get5 Carboxyl-terminal Domain Is a Novel Dimerization Motif That Tethers an Extended Get4/Get5 Complex

Chartron, Justin W. and VanderVelde, David G. and Rao, Meera and Clemons, William M., Jr. (2012) Get5 Carboxyl-terminal Domain Is a Novel Dimerization Motif That Tethers an Extended Get4/Get5 Complex. Journal of Biological Chemistry, 287 (11). pp. 8310-8317. ISSN 0021-9258. PMCID PMC3318709. doi:10.1074/jbc.M111.333252. https://resolver.caltech.edu/CaltechAUTHORS:20120410-081219219

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Abstract

Tail-anchored trans-membrane proteins are targeted to membranes post-translationally. The proteins Get4 and Get5 form an obligate complex that catalyzes the transfer of tail-anchored proteins destined to the endoplasmic reticulum from Sgt2 to the cytosolic targeting factor Get3. Get5 forms a homodimer mediated by its carboxyl domain. We show here that a conserved motif exists within the carboxyl domain. A high resolution crystal structure and solution NMR structures of this motif reveal a novel and stable helical dimerization domain. We additionally determined a solution NMR structure of a divergent fungal homolog, and comparison of these structures allows annotation of specific stabilizing interactions. Using solution x-ray scattering and the structures of all folded domains, we present a model of the full-length Get4/Get5 complex.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1074/jbc.M111.333252 DOIArticle
http://www.jbc.org/content/287/11/8310PublisherArticle
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3318709/PubMed CentralArticle
ORCID:
AuthorORCID
VanderVelde, David G.0000-0002-2907-0366
Clemons, William M., Jr.0000-0002-0021-889X
Additional Information:© 2012 by The American Society for Biochemistry and Molecular Biology, Inc. Received for publication, December 12, 2011, and in revised form, January 3, 2012 Published, JBC Papers in Press, January 17, 2012. The Molecular Observatory at Caltech is supported by the Gordon and Betty Moore Foundation, the Beckman Institute, and the Sanofi-Aventis Bioengineering Research Program. Operations at SSRL are supported by the United States Department of Energy and the National Institutes of Health. Supported by National Institutes of Health Grant R01GM097572, the Searle Scholar program, and a Burroughs-Wellcome Fund career award for the biological sciences. We thank S. O. Shan, M. E. Rome, C. J. M. Suloway, and H. B. Gristick for critical reading of the manuscript; members of the laboratory for support and useful discussions; Julie Hoy for help in data collection on our home source; Graeme Card, Ana Gonzalez, and Michael Soltice for help with data collection at SSRL BL12-2; and Tsutomu Matsui and Hiro Tsuruta (1962–August 2011) for help with bioSAXS data collection and processing at SSRL BL4-2.
Funders:
Funding AgencyGrant Number
Gordon and Betty Moore FoundationUNSPECIFIED
Caltech Beckman InstituteUNSPECIFIED
Sanofi-Aventis Bioengineering Research ProgramUNSPECIFIED
Department of Energy (DOE)UNSPECIFIED
NIHR01GM097572
Searle Scholars ProgramUNSPECIFIED
Burroughs-Wellcome FundUNSPECIFIED
Issue or Number:11
PubMed Central ID:PMC3318709
DOI:10.1074/jbc.M111.333252
Record Number:CaltechAUTHORS:20120410-081219219
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20120410-081219219
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:30044
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:10 Apr 2012 21:40
Last Modified:09 Nov 2021 19:35

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