Allosteric regulation of Hsp70 chaperones by a proline switch - PubMed (original) (raw)
Allosteric regulation of Hsp70 chaperones by a proline switch
Markus Vogel et al. Mol Cell. 2006.
Free article
Abstract
Crucial to the function of Hsp70 chaperones is the nucleotide-regulated transition between two conformational states, the ATP bound state with high association and dissociation rates for substrates and the ADP bound state with two and three orders of magnitude lower association and dissociation rates. The spontaneous transition between the two states is extremely slow, indicating a high energy barrier for the switch that regulates the transition. Here we provide evidence that a universally conserved proline in the ATPase domain constitutes the switch that assumes alternate conformations in response to ATP binding and hydrolysis. The conformation of the proline, acting through an invariant arginine as relay, determines and stabilizes the opened and closed conformation of the substrate binding domain and thereby regulates the chaperone activity of Hsp70.
Similar articles
- The second metal-binding site of 70 kDa heat-shock protein is essential for ADP binding, ATP hydrolysis and ATP synthesis.
Wu X, Yano M, Washida H, Kido H. Wu X, et al. Biochem J. 2004 Mar 15;378(Pt 3):793-9. doi: 10.1042/BJ20031680. Biochem J. 2004. PMID: 14664695 Free PMC article. - Multistep mechanism of substrate binding determines chaperone activity of Hsp70.
Mayer MP, Schröder H, Rüdiger S, Paal K, Laufen T, Bukau B. Mayer MP, et al. Nat Struct Biol. 2000 Jul;7(7):586-93. doi: 10.1038/76819. Nat Struct Biol. 2000. PMID: 10876246 - Interdomain communication in the molecular chaperone DnaK.
Han W, Christen P. Han W, et al. Biochem J. 2003 Feb 1;369(Pt 3):627-34. doi: 10.1042/BJ20020943. Biochem J. 2003. PMID: 12383055 Free PMC article. - Mechanism of substrate recognition by Hsp70 chaperones.
Erbse A, Mayer MP, Bukau B. Erbse A, et al. Biochem Soc Trans. 2004 Aug;32(Pt 4):617-21. doi: 10.1042/BST0320617. Biochem Soc Trans. 2004. PMID: 15270690 Review. - The mechanism of Hsp70 chaperones: (entropic) pulling the models together.
Goloubinoff P, De Los Rios P. Goloubinoff P, et al. Trends Biochem Sci. 2007 Aug;32(8):372-80. doi: 10.1016/j.tibs.2007.06.008. Epub 2007 Jul 12. Trends Biochem Sci. 2007. PMID: 17629485 Review.
Cited by
- Tau local structure shields an amyloid-forming motif and controls aggregation propensity.
Chen D, Drombosky KW, Hou Z, Sari L, Kashmer OM, Ryder BD, Perez VA, Woodard DR, Lin MM, Diamond MI, Joachimiak LA. Chen D, et al. Nat Commun. 2019 Jun 7;10(1):2493. doi: 10.1038/s41467-019-10355-1. Nat Commun. 2019. PMID: 31175300 Free PMC article. - The Hsp70-Chaperone Machines in Bacteria.
Mayer MP. Mayer MP. Front Mol Biosci. 2021 Jun 7;8:694012. doi: 10.3389/fmolb.2021.694012. eCollection 2021. Front Mol Biosci. 2021. PMID: 34164436 Free PMC article. Review. - ATP-induced conformational changes in Hsp70: molecular dynamics and experimental validation of an in silico predicted conformation.
Woo HJ, Jiang J, Lafer EM, Sousa R. Woo HJ, et al. Biochemistry. 2009 Dec 8;48(48):11470-7. doi: 10.1021/bi901256y. Biochemistry. 2009. PMID: 19883127 Free PMC article. - Pharmacological targeting of the Hsp70 chaperone.
Patury S, Miyata Y, Gestwicki JE. Patury S, et al. Curr Top Med Chem. 2009;9(15):1337-51. doi: 10.2174/156802609789895674. Curr Top Med Chem. 2009. PMID: 19860737 Free PMC article. Review. - J-domain proteins promote client relay from Hsp70 during tail-anchored membrane protein targeting.
Cho H, Shim WJ, Liu Y, Shan SO. Cho H, et al. J Biol Chem. 2021 Jan-Jun;296:100546. doi: 10.1016/j.jbc.2021.100546. Epub 2021 Mar 17. J Biol Chem. 2021. PMID: 33741343 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources