T-complex protein Ring Complex (TRiC), otherwise known as Chaperonin Containing TCP-1 (CCT),[a] is a multiprotein complex and the chaperonin of eukaryotic cells. Like the bacterial GroEL, the TRiC complex aids in the folding of ~10% of the proteome, and actin and tubulin are some of its best known substrates.[2][3] TRiC is an example of a biological machine that folds substrates within the central cavity of its barrel-like assembly using the energy from ATP hydrolysis.
Structure of Saccharomyces cerevisiae TRiC in the AMP-PNP bound state (PDB 5GW5).[1]
The human TRiC complex is formed by two rings containing 8 similar but non-identical subunits, each with molecular weights of ~60 kDa. The two rings are stacked in an asymmetrical fashion, forming a barrel-like structure with a molecular weight of ~1 MDa.[2][3]
Counterclockwise from the exterior, each ring is made of the subunits in the following order: 6-8-7-5-2-4-1-3.[4]
Evolutionedit
This section is missing information about phylogeny (template) and evolutionary trajectory (pic). Please expand the section to include this information. Further details may exist on the talk page.(December 2020)
The CCT evolved from the archaeal thermosome ~2Gya, with the two subunits diversifying into multiple units. The CCT changed from having one type of subunit, to having two, three, five, and finally eight types.[4]: fig. 4
^The term "TCP-1" is variously expanded as "T-complex protein 1" and "tailless complex polypeptide 1". The "T-complex" is the same as tailless complex, a CCT locus associated with tail length in mice.
Referencesedit
^Zang, Yunxiang; Jin, Mingliang; Wang, Huping; Cui, Zhicheng; Kong, Liangliang; Liu, Caixuan; Cong, Yao (2016-10-24). "Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM". Nature Structural & Molecular Biology. Springer Science and Business Media LLC. 23 (12): 1083–1091. doi:10.1038/nsmb.3309. ISSN 1545-9993. PMID 27775711. S2CID 12001964.
^ abBalchin, David; Hayer-Hartl, Manajit; Hartl, F. Ulrich (2016-06-30). "In vivo aspects of protein folding and quality control". Science. American Association for the Advancement of Science (AAAS). 353 (6294): aac4354. doi:10.1126/science.aac4354. hdl:11858/00-001M-0000-002B-0856-C. ISSN 0036-8075. PMID 27365453. S2CID 5174431.
^ abGestaut, Daniel; Limatola, Antonio; Joachimiak, Lukasz; Frydman, Judith (2019). "The ATP-powered gymnastics of TRiC/CCT: an asymmetric protein folding machine with a symmetric origin story". Current Opinion in Structural Biology. Elsevier BV. 55: 50–58. doi:10.1016/j.sbi.2019.03.002. ISSN 0959-440X. PMC6776438. PMID 30978594.
^ abWillison, KR (5 October 2018). "The structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring". The Biochemical Journal. 475 (19): 3009–3034. doi:10.1042/BCJ20170378. hdl:10044/1/63924. PMID 30291170. S2CID 52923821.
tric, complex, complex, protein, ring, complex, tric, otherwise, known, chaperonin, containing, multiprotein, complex, chaperonin, eukaryotic, cells, like, bacterial, groel, tric, complex, aids, folding, proteome, actin, tubulin, some, best, known, substrates,. T complex protein Ring Complex TRiC otherwise known as Chaperonin Containing TCP 1 CCT a is a multiprotein complex and the chaperonin of eukaryotic cells Like the bacterial GroEL the TRiC complex aids in the folding of 10 of the proteome and actin and tubulin are some of its best known substrates 2 3 TRiC is an example of a biological machine that folds substrates within the central cavity of its barrel like assembly using the energy from ATP hydrolysis Structure of Saccharomyces cerevisiae TRiC in the AMP PNP bound state PDB 5GW5 1 Contents 1 Subunits 2 Evolution 3 See also 4 Notes 5 ReferencesSubunits editThe human TRiC complex is formed by two rings containing 8 similar but non identical subunits each with molecular weights of 60 kDa The two rings are stacked in an asymmetrical fashion forming a barrel like structure with a molecular weight of 1 MDa 2 3 Subunit MW kDa A FeaturesTCP1 CCT1 a 60CCT2 b 57CCT3 g 61CCT4 d 58CCT5 e 60CCT6 z 58 Two copies in human genome CCT6A and CCT6B CCT7 h 59CCT8 8 60A Molecular weight of human subunits Counterclockwise from the exterior each ring is made of the subunits in the following order 6 8 7 5 2 4 1 3 4 Evolution editThis section is missing information about phylogeny template and evolutionary trajectory pic Please expand the section to include this information Further details may exist on the talk page December 2020 The CCT evolved from the archaeal thermosome 2Gya with the two subunits diversifying into multiple units The CCT changed from having one type of subunit to having two three five and finally eight types 4 fig 4 See also editChaperone Chaperonin Heat shock proteinNotes edit The term TCP 1 is variously expanded as T complex protein 1 and tailless complex polypeptide 1 The T complex is the same as tailless complex a CCT locus associated with tail length in mice References edit Zang Yunxiang Jin Mingliang Wang Huping Cui Zhicheng Kong Liangliang Liu Caixuan Cong Yao 2016 10 24 Staggered ATP binding mechanism of eukaryotic chaperonin TRiC CCT revealed through high resolution cryo EM Nature Structural amp Molecular Biology Springer Science and Business Media LLC 23 12 1083 1091 doi 10 1038 nsmb 3309 ISSN 1545 9993 PMID 27775711 S2CID 12001964 a b Balchin David Hayer Hartl Manajit Hartl F Ulrich 2016 06 30 In vivo aspects of protein folding and quality control Science American Association for the Advancement of Science AAAS 353 6294 aac4354 doi 10 1126 science aac4354 hdl 11858 00 001M 0000 002B 0856 C ISSN 0036 8075 PMID 27365453 S2CID 5174431 a b Gestaut Daniel Limatola Antonio Joachimiak Lukasz Frydman Judith 2019 The ATP powered gymnastics of TRiC CCT an asymmetric protein folding machine with a symmetric origin story Current Opinion in Structural Biology Elsevier BV 55 50 58 doi 10 1016 j sbi 2019 03 002 ISSN 0959 440X PMC 6776438 PMID 30978594 a b Willison KR 5 October 2018 The structure and evolution of eukaryotic chaperonin containing TCP 1 and its mechanism that folds actin into a protein spring The Biochemical Journal 475 19 3009 3034 doi 10 1042 BCJ20170378 hdl 10044 1 63924 PMID 30291170 S2CID 52923821 Portal nbsp Biology Retrieved from https en wikipedia org w index php title TRiC complex amp oldid 1122119066, wikipedia, wiki, book, books, library,
