National Institutes of Health/National Center for Advancing Translational Sciences (NIH/NCATS)
UL1TR000445
米国
National Institutes of Health/National Human Genome Research Institute (NIH/NHGRI)
P41GM103832
米国
National Institutes of Health/National Human Genome Research Institute (NIH/NHGRI)
P01NS092525
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM007347
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM074074
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM103124
米国
National Institutes of Health/National Center for Advancing Translational Sciences (NIH/NCATS)
UL1TR000445
米国
European Research Council (ERC)
AdvG 233226
European Union
European Research Council (ERC)
AdvG 670821
European Union
引用
ジャーナル: Proc Natl Acad Sci U S A / 年: 2021 タイトル: Structural and functional dissection of reovirus capsid folding and assembly by the prefoldin-TRiC/CCT chaperone network. 著者: Jonathan J Knowlton / Daniel Gestaut / Boxue Ma / Gwen Taylor / Alpay Burak Seven / Alexander Leitner / Gregory J Wilson / Sreejesh Shanker / Nathan A Yates / B V Venkataram Prasad / Ruedi ...著者: Jonathan J Knowlton / Daniel Gestaut / Boxue Ma / Gwen Taylor / Alpay Burak Seven / Alexander Leitner / Gregory J Wilson / Sreejesh Shanker / Nathan A Yates / B V Venkataram Prasad / Ruedi Aebersold / Wah Chiu / Judith Frydman / Terence S Dermody / 要旨: 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 ...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, cross-linking 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 the molecular 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.