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TitlePathway of Actin Folding Directed by the Eukaryotic Chaperonin TRiC.
Journal, issue, pagesCell, Vol. 174, Issue 6, Page 1507-1521.e16, Year 2018
Publish dateSep 6, 2018
AuthorsDavid Balchin / Goran Miličić / Mike Strauss / Manajit Hayer-Hartl / F Ulrich Hartl /
PubMed AbstractThe hetero-oligomeric chaperonin of eukarya, TRiC, is required to fold the cytoskeletal protein actin. The simpler bacterial chaperonin system, GroEL/GroES, is unable to mediate actin folding. Here, ...The hetero-oligomeric chaperonin of eukarya, TRiC, is required to fold the cytoskeletal protein actin. The simpler bacterial chaperonin system, GroEL/GroES, is unable to mediate actin folding. Here, we use spectroscopic and structural techniques to determine how TRiC promotes the conformational progression of actin to the native state. We find that actin fails to fold spontaneously even in the absence of aggregation but populates a kinetically trapped, conformationally dynamic state. Binding of this frustrated intermediate to TRiC specifies an extended topology of actin with native-like secondary structure. In contrast, GroEL stabilizes bound actin in an unfolded state. ATP binding to TRiC effects an asymmetric conformational change in the chaperonin ring. This step induces the partial release of actin, priming it for folding upon complete release into the chaperonin cavity, mediated by ATP hydrolysis. Our results reveal how the unique features of TRiC direct the folding pathway of an obligate eukaryotic substrate.
External linksCell / PubMed:30100183
MethodsEM (single particle)
Resolution7.6 - 16.7 Å
Structure data

EMDB-0015:
Symmetry-free cryo-EM map of GroEL-actin
Method: EM (single particle) / Resolution: 10.3 Å

EMDB-0016:
Symmetry-free cryo-EM map of TRiC in apo state (nucleotide free)
Method: EM (single particle) / Resolution: 8.8 Å

EMDB-0017:
Symmetry-free cryo-EM map of TRiC-actin
Method: EM (single particle) / Resolution: 9.1 Å

EMDB-0018:
Symmetry-free cryo-EM map of TRiC-actin-alpha_CCT1
Method: EM (single particle) / Resolution: 16.7 Å

EMDB-0022:
Symmetry-free cryo-EM map of TRiC-ADP-BeFx
Method: EM (single particle) / Resolution: 7.6 Å

Source
  • Escherichia coli (E. coli)
  • Bos taurus (cattle)

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