气候变化领域集成服务门户(CCPortal): Structural and functional dissection of reovirus capsid folding and assembly by the prefoldin-TRiC/CCT chaperone network

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DOI	10.1073/pnas.2018127118
	Structural and functional dissection of reovirus capsid folding and assembly by the prefoldin-TRiC/CCT chaperone network
	Knowlton J.J.; Gestaut D.; Ma B.; Taylor G.; Seven A.B.; Leitner A.; Wilsonk G.J.; Shanker S.; Yates N.A.; B. V. Venkataram Prasad; Aebersold R.; Chiu W.; Frydman J.; Dermody T.S.
发表日期	2021
ISSN	00278424
卷号	118 期号:11
英文摘要	Intracellular protein homeostasis is maintained by a network of chaperones that function to fold proteins into their native conformation. The eukaryotic TRiC chaperonin (TCP1-ring complex, also called CCT for cytosolic chaperonin containing TCP1) facilitates folding of a subset of proteins with folding constraints such as complex topologies. To better understand the mechanism of TRiC folding, we investigated the biogenesis of an obligate TRiC substrate, the reovirus σ3 capsid protein. We discovered that the σ3 protein interacts with a network of chaperones, including TRiC and prefoldin. Using a combination of cryoelectron microscopy, crosslinking mass spectrometry, and biochemical approaches, we establish functions for TRiC and prefoldin in folding σ3 and promoting its assembly into higher-order oligomers. These studies illuminate themolecular dynamics of σ3 folding and establish a biological function for TRiC in virus assembly. In addition, our findings provide structural and functional insight into the mechanism by which TRiC and prefoldin participate in the assembly of protein complexes. © 2021 National Academy of Sciences. All rights reserved.
英文关键词	Molecular chaperones; Prefoldin; Protein folding; TRiC; Virus assembly
语种	英语
scopus关键词	capsid protein; chaperone; prefoldin; TRiC protein; unclassified drug; Article; complex formation; crosslinking mass spectrometry; cryoelectron microscopy; enzyme substrate; mass spectrometry; molecular dynamics; nonhuman; priority journal; protein assembly; protein folding; protein function; protein interaction; protein localization; protein structure; Reoviridae; virus assembly
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/180274
作者单位	Department of Pediatrics, University of Pittsburgh School of Medicine, Pittsburgh, PA 15224, United States; Department of Pathology, Microbiology, and Immunology, Vanderbilt University Medical Center, Nashville, TN 37232, United States; Department of Biology, Stanford University, Stanford, CA 94305, United States; Department of Bioengineering, Stanford University, Stanford, CA 94305, United States; Department of Microbiology and Immunology, Stanford University, Stanford, CA 94305, United States; Department of Photon Science, Stanford University, Stanford, CA 94305, United States; Center for Microbial Pathogenesis, UPMC Children's Hospital of Pittsburgh, Pittsburgh, PA 15224, United States; Department of Structural Biology, Stanford University, Stanford, CA 94305, United States; Department of Molecular and Cellular Physiology, Stanford University, Palo Alto, CA 94305, United States; Department of Biology, Institute of Molecular Systems Biology, ETH Zürich, Zürich, 8093, Switzerland; Department of ...
推荐引用方式 GB/T 7714	Knowlton J.J.,Gestaut D.,Ma B.,et al. Structural and functional dissection of reovirus capsid folding and assembly by the prefoldin-TRiC/CCT chaperone network[J],2021,118(11).
APA	Knowlton J.J..,Gestaut D..,Ma B..,Taylor G..,Seven A.B..,...&Dermody T.S..(2021).Structural and functional dissection of reovirus capsid folding and assembly by the prefoldin-TRiC/CCT chaperone network.Proceedings of the National Academy of Sciences of the United States of America,118(11).
MLA	Knowlton J.J.,et al."Structural and functional dissection of reovirus capsid folding and assembly by the prefoldin-TRiC/CCT chaperone network".Proceedings of the National Academy of Sciences of the United States of America 118.11(2021).