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TitleStructural visualization of the tubulin folding pathway directed by human chaperonin TRiC/CCT.
Journal, issue, pagesCell, Vol. 185, Issue 25, Page 4770-4787.e20, Year 2022
Publish dateDec 8, 2022
AuthorsDaniel Gestaut / Yanyan Zhao / Junsun Park / Boxue Ma / Alexander Leitner / Miranda Collier / Grigore Pintilie / Soung-Hun Roh / Wah Chiu / Judith Frydman /
PubMed AbstractThe ATP-dependent ring-shaped chaperonin TRiC/CCT is essential for cellular proteostasis. To uncover why some eukaryotic proteins can only fold with TRiC assistance, we reconstituted the folding of ...The ATP-dependent ring-shaped chaperonin TRiC/CCT is essential for cellular proteostasis. To uncover why some eukaryotic proteins can only fold with TRiC assistance, we reconstituted the folding of β-tubulin using human prefoldin and TRiC. We find unstructured β-tubulin is delivered by prefoldin to the open TRiC chamber followed by ATP-dependent chamber closure. Cryo-EM resolves four near-atomic-resolution structures containing progressively folded β-tubulin intermediates within the closed TRiC chamber, culminating in native tubulin. This substrate folding pathway appears closely guided by site-specific interactions with conserved regions in the TRiC chamber. Initial electrostatic interactions between the TRiC interior wall and both the folded tubulin N domain and its C-terminal E-hook tail establish the native substrate topology, thus enabling C-domain folding. Intrinsically disordered CCT C termini within the chamber promote subsequent folding of tubulin's core and middle domains and GTP-binding. Thus, TRiC's chamber provides chemical and topological directives that shape the folding landscape of its obligate substrates.
External linksCell / PubMed:36493755 / PubMed Central
MethodsEM (single particle)
Resolution2.9 - 3.85 Å
Structure data

26089

7trg

EMDB-26089, PDB-7trg:
The beta-tubulin folding intermediate I
Method: EM (single particle) / Resolution: 3.0 Å

26120

7ttn

EMDB-26120, PDB-7ttn:
The beta-tubulin folding intermediate II
Method: EM (single particle) / Resolution: 3.3 Å

26123

7ttt

EMDB-26123, PDB-7ttt:
The beta-tubulin folding intermediate III
Method: EM (single particle) / Resolution: 2.9 Å

26131

7tub

EMDB-26131, PDB-7tub:
The beta-tubulin folding intermediate IV
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-32822: An apo TRiC map
Method: EM (single particle) / Resolution: 3.11 Å

32823

7wu7

EMDB-32823, PDB-7wu7:
Prefoldin-tubulin-TRiC complex
Method: EM (single particle) / Resolution: 3.85 Å

Chemicals

ChemComp-MG:
Unknown entry

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

ChemComp-AF3:
ALUMINUM FLUORIDE / Aluminium fluoride

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
KeywordsCHAPERONE / Human chaperonin TRiC with beta-tubulin folding intermediate I / Human chaperonin TRiC with beta-tubulin folding intermediate II / Human chaperonin TRiC with beta-tubulin folding intermediate III / Human chaperonin TRiC with beta-tubulin folding intermediate IV / chapronin complex

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