zona pellucida receptor complex / positive regulation of establishment of protein localization to telomere / positive regulation of protein localization to Cajal body / scaRNA localization to Cajal body / positive regulation of telomerase RNA localization to Cajal body / symbiont-mediated suppression of host PKR/eIFalpha signaling / tubulin complex assembly / chaperonin-containing T-complex / : / BBSome-mediated cargo-targeting to cilium ...zona pellucida receptor complex / positive regulation of establishment of protein localization to telomere / positive regulation of protein localization to Cajal body / scaRNA localization to Cajal body / positive regulation of telomerase RNA localization to Cajal body / symbiont-mediated suppression of host PKR/eIFalpha signaling / tubulin complex assembly / chaperonin-containing T-complex / : / BBSome-mediated cargo-targeting to cilium / viral outer capsid / Formation of tubulin folding intermediates by CCT/TriC / binding of sperm to zona pellucida / Folding of actin by CCT/TriC / Prefoldin mediated transfer of substrate to CCT/TriC / RHOBTB1 GTPase cycle / WD40-repeat domain binding / pericentriolar material / Association of TriC/CCT with target proteins during biosynthesis / protein serine/threonine kinase inhibitor activity / beta-tubulin binding / chaperone-mediated protein complex assembly / 加水分解酵素; 酸無水物に作用; リン含有酸無水物に作用 / RHOBTB2 GTPase cycle / heterochromatin / : / viral life cycle / positive regulation of telomere maintenance via telomerase / protein folding chaperone / acrosomal vesicle / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / mRNA 3'-UTR binding / cell projection / ATP-dependent protein folding chaperone / mRNA 5'-UTR binding / response to virus / azurophil granule lumen / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / unfolded protein binding / melanosome / protein folding / G-protein beta-subunit binding / regulation of translation / cell body / secretory granule lumen / ficolin-1-rich granule lumen / microtubule / host cell cytoplasm / cytoskeleton / protein stabilization / cilium / symbiont-mediated suppression of host innate immune response / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / cadherin binding / ubiquitin protein ligase binding / centrosome / Neutrophil degranulation / host cell nucleus / structural molecule activity / Golgi apparatus / ATP hydrolysis activity / RNA binding / extracellular exosome / extracellular region / zinc ion binding / nucleoplasm / ATP binding / identical protein 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.