Abstract:
: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 CCT beta 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.
journal_name
Nat Struct Mol Bioljournal_title
Nature structural & molecular biologyauthors
Cuéllar J,Martín-Benito J,Scheres SH,Sousa R,Moro F,López-Viñas E,Gómez-Puertas P,Muga A,Carrascosa JL,Valpuesta JMdoi
10.1038/nsmb.1464subject
Has Abstractpub_date
2008-08-01 00:00:00pages
858-64issue
8eissn
1545-9993issn
1545-9985pii
nsmb.1464journal_volume
15pub_type
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