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Structure paper

TitleRPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex.
Journal, issue, pagesNat Commun, Vol. 9, Issue 1, Page 1501, Year 2018
Publish dateApr 16, 2018
AuthorsFabrizio Martino / Mohinder Pal / Hugo Muñoz-Hernández / Carlos F Rodríguez / Rafael Núñez-Ramírez / David Gil-Carton / Gianluca Degliesposti / J Mark Skehel / S Mark Roe / Chrisostomos Prodromou / Laurence H Pearl / Oscar Llorca /
PubMed AbstractThe R2TP/Prefoldin-like co-chaperone, in concert with HSP90, facilitates assembly and cellular stability of RNA polymerase II, and complexes of PI3-kinase-like kinases such as mTOR. However, the ...The R2TP/Prefoldin-like co-chaperone, in concert with HSP90, facilitates assembly and cellular stability of RNA polymerase II, and complexes of PI3-kinase-like kinases such as mTOR. However, the mechanism by which this occurs is poorly understood. Here we use cryo-EM and biochemical studies on the human R2TP core (RUVBL1-RUVBL2-RPAP3-PIH1D1) which reveal the distinctive role of RPAP3, distinguishing metazoan R2TP from the smaller yeast equivalent. RPAP3 spans both faces of a single RUVBL ring, providing an extended scaffold that recruits clients and provides a flexible tether for HSP90. A 3.6 Å cryo-EM structure reveals direct interaction of a C-terminal domain of RPAP3 and the ATPase domain of RUVBL2, necessary for human R2TP assembly but absent from yeast. The mobile TPR domains of RPAP3 map to the opposite face of the ring, associating with PIH1D1, which mediates client protein recruitment. Thus, RPAP3 provides a flexible platform for bringing HSP90 into proximity with diverse client proteins.
External linksNat Commun / PubMed:29662061 / PubMed Central
MethodsEM (single particle)
Resolution3.57 - 8.72 Å
Structure data

4287

6fo1

EMDB-4287, PDB-6fo1:
Human R2TP subcomplex containing 1 RUVBL1-RUVBL2 hexamer bound to 1 RBD domain from RPAP3.
Method: EM (single particle) / Resolution: 3.57 Å

EMDB-4289:
Human R2TP complex-C3symmetry
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-4290:
Human R2TP complex-subcomplex1
Method: EM (single particle) / Resolution: 8.72 Å

EMDB-4291:
Human R2TP complex-subgroup2
Method: EM (single particle) / Resolution: 6.57 Å

Chemicals

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

Source
  • homo sapiens (human)
KeywordsCHAPERONE / R2TP / HSP90 co-chaperone / PIH1D1 / RPAP3 / RUVBL1-RUVBL2

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