zona pellucida receptor complex / scaRNA localization to Cajal body / symbiont-mediated suppression of host PKR/eIFalpha signaling / chaperone mediated protein folding independent of cofactor / viral outer capsid / positive regulation of establishment of protein localization to telomere / positive regulation of protein localization to Cajal body / tubulin complex assembly / BBSome-mediated cargo-targeting to cilium / Folding of actin by CCT/TriC ...zona pellucida receptor complex / scaRNA localization to Cajal body / symbiont-mediated suppression of host PKR/eIFalpha signaling / chaperone mediated protein folding independent of cofactor / viral outer capsid / positive regulation of establishment of protein localization to telomere / positive regulation of protein localization to Cajal body / tubulin complex assembly / BBSome-mediated cargo-targeting to cilium / Folding of actin by CCT/TriC / binding of sperm to zona pellucida / Formation of tubulin folding intermediates by CCT/TriC / positive regulation of telomerase RNA localization to Cajal body / Prefoldin mediated transfer of substrate to CCT/TriC / chaperonin-containing T-complex / protein serine/threonine kinase inhibitor activity / RHOBTB1 GTPase cycle / intermediate filament cytoskeleton / WD40-repeat domain binding / pericentriolar material / beta-tubulin binding / Association of TriC/CCT with target proteins during biosynthesis / chaperone-mediated protein complex assembly / RHOBTB2 GTPase cycle / heterochromatin / chaperone-mediated protein folding / protein folding chaperone / positive regulation of telomerase activity / viral life cycle / positive regulation of telomere maintenance via telomerase / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / acrosomal vesicle / mRNA 3'-UTR binding / cell projection / ATP-dependent protein folding chaperone / response to virus / mRNA 5'-UTR binding / cilium / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / G-protein beta-subunit binding / azurophil granule lumen / unfolded protein binding / melanosome / protein folding / regulation of translation / cell body / secretory granule lumen / microtubule / ficolin-1-rich granule lumen / host cell cytoplasm / cytoskeleton / protein stabilization / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / cadherin binding / virus-mediated perturbation of host defense response / centrosome / ubiquitin protein ligase binding / host cell nucleus / Neutrophil degranulation / structural molecule activity / Golgi apparatus / ATP hydrolysis activity / RNA binding / extracellular exosome / extracellular region / nucleoplasm / ATP binding / metal ion binding / cytoplasm / cytosol 類似検索 - 分子機能
Reovirus, outer capsid sigma 3 / Reovirus, outer capsid sigma-3 domain superfamily / Reovirus outer capsid protein, Sigma 3 / T-complex protein 1, alpha subunit / T-complex protein 1, eta subunit / T-complex protein 1, theta subunit / T-complex protein 1, zeta subunit / T-complex protein 1, delta subunit / T-complex protein 1, gamma subunit / T-complex protein 1, epsilon subunit ...Reovirus, outer capsid sigma 3 / Reovirus, outer capsid sigma-3 domain superfamily / Reovirus outer capsid protein, Sigma 3 / T-complex protein 1, alpha subunit / T-complex protein 1, eta subunit / T-complex protein 1, theta subunit / T-complex protein 1, zeta subunit / T-complex protein 1, delta subunit / T-complex protein 1, gamma subunit / T-complex protein 1, epsilon subunit / T-complex protein 1, beta subunit / Chaperonins TCP-1 signature 1. / Chaperonins TCP-1 signature 2. / Chaperonin TCP-1, conserved site / Chaperonins TCP-1 signature 3. / Chaperone tailless complex polypeptide 1 (TCP-1) / GroEL-like equatorial domain superfamily / TCP-1-like chaperonin intermediate domain superfamily / GroEL-like apical domain superfamily / TCP-1/cpn60 chaperonin family / Chaperonin Cpn60/GroEL/TCP-1 family 類似検索 - ドメイン・相同性
Outer capsid protein sigma-3 / T-complex protein 1 subunit alpha / T-complex protein 1 subunit zeta / T-complex protein 1 subunit epsilon / T-complex protein 1 subunit gamma / T-complex protein 1 subunit theta / T-complex protein 1 subunit delta / T-complex protein 1 subunit beta / T-complex protein 1 subunit eta 類似検索 - 構成要素
生物種
Homo sapiens (ヒト) / Mammalian orthoreovirus 3 Dearing (ウイルス) / Reovirus type 3 (strain Dearing) (ウイルス)
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.