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Structure paper

TitleStructural basis of plp2-mediated cytoskeletal protein folding by TRiC/CCT.
Journal, issue, pagesSci Adv, Vol. 9, Issue 11, Page eade1207, Year 2023
Publish dateMar 17, 2023
AuthorsWenyu Han / Mingliang Jin / Caixuan Liu / Qiaoyu Zhao / Shutian Wang / Yifan Wang / Yue Yin / Chao Peng / Yanxing Wang / Yao Cong /
PubMed AbstractThe cytoskeletal proteins tubulin and actin are the obligate substrates of TCP-1 ring complex/Chaperonin containing TCP-1 (TRiC/CCT), and their folding involves co-chaperone. Through cryo-electron ...The cytoskeletal proteins tubulin and actin are the obligate substrates of TCP-1 ring complex/Chaperonin containing TCP-1 (TRiC/CCT), and their folding involves co-chaperone. Through cryo-electron microscopy analysis, we present a more complete picture of TRiC-assisted tubulin/actin folding along TRiC adenosine triphosphatase cycle, under the coordination of co-chaperone plp2. In the open S1/S2 states, plp2 and tubulin/actin engaged within opposite TRiC chambers. Notably, we captured an unprecedented TRiC-plp2-tubulin complex in the closed S3 state, engaged with a folded full-length -tubulin and loaded with a guanosine triphosphate, and a plp2 occupying opposite rings. Another closed S4 state revealed an actin in the intermediate folding state and a plp2. Accompanying TRiC ring closure, plp2 translocation could coordinate substrate translocation on the CCT6 hemisphere, facilitating substrate stabilization and folding. Our findings reveal the folding mechanism of the major cytoskeletal proteins tubulin/actin under the coordination of the biogenesis machinery TRiC and plp2 and extend our understanding of the links between cytoskeletal proteostasis and related human diseases.
External linksSci Adv / PubMed:36921056 / PubMed Central
MethodsEM (single particle)
Resolution3.05 - 4.55 Å
Structure data

33917

7ylu

EMDB-33917, PDB-7ylu:
yeast TRiC-plp2-substrate complex at S1 TRiC-NPP state
Method: EM (single particle) / Resolution: 4.55 Å

33918

7ylv

EMDB-33918, PDB-7ylv:
yeast TRiC-plp2-substrate complex at S2 ATP binding state
Method: EM (single particle) / Resolution: 3.91 Å

33919

7ylw

EMDB-33919, PDB-7ylw:
yeast TRiC-plp2-tubulin complex at S3 closed TRiC state
Method: EM (single particle) / Resolution: 3.39 Å

33920

7ylx

EMDB-33920, PDB-7ylx:
yeast TRiC-plp2-actin complex at S4 closed TRiC state
Method: EM (single particle) / Resolution: 3.2 Å

33921

7yly

EMDB-33921, PDB-7yly:
yeast TRiC-plp2 complex at S5 closed TRiC state
Method: EM (single particle) / Resolution: 3.05 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-AF3:
ALUMINUM FLUORIDE

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

ChemComp-HOH:
WATER

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsCHAPERONE / TRiC/CCT / phosducin-like protein / tubulin / actin

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