The structure of CCT-Hsc70NBD suggests a mechanism for Hsp70 delivery of substrates to the chaperonin

Jorge Cuéllar, Jaime Martín-Benito, Sjors H.W. Scheres, Rui Sousa, Fernando Moro, Eduardo López-Vĩas, Paulino Gómez-Puertas, Arturo Muga, José L. Carrascosa, José M. Valpuesta

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70 Scopus citations


Chaperones, a group of proteins that assist the folding of other proteins, seem to work in a coordinated manner. Two major chaperone families are heat-shock protein families Hsp60 and Hsp70. Here we show for the first time the formation of a stable complex between chaperonin-containing TCP-1 (CCT) and Hsc70, two eukaryotic representatives of these chaperone families. This interaction takes place between the apical domain of the CCTΒ subunit and the nucleotide binding domain of Hsc70, and may serve to deliver the unfolded substrate from Hsc70 to the substrate binding region of CCT. We also show that a similar interaction does not occur between their prokaryotic counterparts GroEL and DnaK, suggesting that in eukarya the two types of chaperones have evolved to a concerted action that makes the folding task more efficient.

Original languageEnglish (US)
Pages (from-to)858-864
Number of pages7
JournalNature Structural and Molecular Biology
Issue number8
StatePublished - Aug 2008

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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