Structural characterization of the substrate transfer mechanism in Hsp70/Hsp90 folding machinery mediated by Hop

• Published in: Nature communications Vol. 5; no. 1; p. 5484
• Main Authors: Alvira, Sara, Cuéllar, Jorge, Röhl, Alina, Yamamoto, Soh, Itoh, Hideaki, Alfonso, Carlos, Rivas, Germán, Buchner, Johannes, Valpuesta, José M.
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 19.11.2014; Nature Publishing Group
• Subjects: 101/28; 631/45/470; 631/45/535; Heat-Shock Proteins - ultrastructure; HSP40 Heat-Shock Proteins - metabolism; HSP70 Heat-Shock Proteins - metabolism; HSP70 Heat-Shock Proteins - ultrastructure; HSP90 Heat-Shock Proteins - metabolism; HSP90 Heat-Shock Proteins - ultrastructure; Humanities and Social Sciences; Humans; Microscopy, Electron; multidisciplinary; Protein Binding; Protein Folding; Protein Structure, Tertiary; Receptors, Glucocorticoid - metabolism; Science; Science (multidisciplinary)

In eukarya, chaperones Hsp70 and Hsp90 act coordinately in the folding and maturation of a range of key proteins with the help of several co-chaperones, especially Hop. Although biochemical data define the Hop-mediated Hsp70–Hsp90 substrate transfer mechanism, the intrinsic flexibility of these prot...