Identification of Regions Involved in Substrate Binding and Dimer Stabilization within the Central Domains of Yeast Hsp40 Sis1

PLoS ONE

Volumn 7, Issue 12, 2012, Pages

  Borges, Júlio C ^a   Seraphim, Thiago V ^a,b   Mokry, David Z ^b   Almeida, Fabio C L ^c   Cyr, Douglas M ^d   Ramos, Carlos H I ^b  

^a UNIVERSITY OF SÃO PAULO   (Brazil)

^b UNIVERSITY OF CAMPINAS   (Brazil)

^c FEDERAL UNIVERSITY OF RIO DE JANEIRO   (Brazil)

^d UNIVERSITY OF NORTH CAROLINA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; GLYCINE; HEAT SHOCK PROTEIN 40; METHIONINE; MONOMER; MUTANT PROTEIN; PROTEIN DNAJ; SIS1 PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; DIFFERENTIAL SCANNING CALORIMETRY; DIMERIZATION; ENZYME SUBSTRATE COMPLEX; FLUORESCENCE; GEL PERMEATION CHROMATOGRAPHY; LIGHT SCATTERING; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN STABILITY; PROTEIN UNFOLDING; THERMODYNAMICS; ULTRACENTRIFUGATION;

AMINO ACID SEQUENCE; BINDING SITES; CALORIMETRY, DIFFERENTIAL SCANNING; CIRCULAR DICHROISM; HSP40 HEAT-SHOCK PROTEINS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTANT PROTEINS; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; PROTEIN STRUCTURE, TERTIARY; PROTEIN UNFOLDING; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SPECTROMETRY, FLUORESCENCE; SUBSTRATE SPECIFICITY; TEMPERATURE; UREA;

EUKARYOTA;

EID: 84870817678     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0050927     Document Type: Article

References (31)

1. Mayer MP, Brehmer D, Gassler CS, Bukau B, (2002) Hsp70 chaperone machines. Adv Protein Chem 59: 1-44.
2. Hartl FU, Hayer-Hartl M, (2002) Protein folding- Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295: 1852-1858.
3. Fan CY, Lee S, Cyr DM, (2003) Mechanisms for regulation of Hsp70 function by Hsp40. Cell Stress Chaperones 8: 309-316.
4. Summers DW, Douglas PM, Ramos CHI, Cyr DM, (2009) Polypeptide transfer from Hsp40 to Hsp70 molecular chaperones. Trends Biochem Sci 34: 230-233.
5. Li J, Qian XG, Sha BD, (2009) Heat shock protein 40: structural studies and their functional implications. Protein Pept Lett 16: 606-612.
6. da Silva KP, Borges JC, (2011) The Molecular Chaperone Hsp70 Family Members Function by a Bidirectional Heterotrophic Allosteric Mechanism. Protein Pept Lett 18: 132-142.
7. Cyr DM, Langer T, Douglas MG, (1994) Dnaj-Like Proteins- Molecular Chaperones and Specific Regulators of Hsp70. Trends Biochem Sci 19: 176-181.
8. Cheetham ME, Caplan AJ, (1998) Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function. Cell Stress Chaperones 3: 28-36.
9. Kampinga HH, Craig EA, (2010) The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat Rev Mol Cell Biol 11 579-592: 10.1038/nrm2941.
10. Young JC, (2010) Mechanisms of the Hsp70 chaperone system. Biochem Cell Biol 88: 291-300.
11. Rudiger S, Schneider-Mergener J, Bukau B, (2001) Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone. EMBO J 20: 1042-1050.
12. Lee S, Fan CY, Younger JM, Ren HY, Cyr DM, (2002) Identification of essential residues in the Type II Hsp40 Sis1 that function in polypeptide binding. J Biol Chem 277: 21675-21682.
13. Li JZ, Oian XG, Sha B, (2003) The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate. Structure 11: 1475-1483.
14. Langer T, Lu C, Echols H, Flanagan J, Hayer MK, et al. (1992) Successive Action of Dnak, Dnaj and Groel Along the Pathway of Chaperone-Mediated Protein Folding. Nature 356: 683-689.
15. Szyperski T, Pellecchia M, Wall D, Georgopoulos C, Wuthrich K, (1994) Nmr Structure Determination of the Escherichia-Coli Dnaj Molecular Chaperone- Secondary Structure and Backbone Fold of the N-Terminal Region (Residues-2-108) Containing the Highly Conserved J-Domain. Proc Natl Acad Sci U S A 91: 11343-11347.
16. Sha BD, Lee S, Cyr DM, (2000) The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1. Structure 8: 799-807.
17. Cyr DM, (1995) Cooperation of the Molecular Chaperone Ydj1 with Specific Hsp70 Homologs to Suppress Protein Aggregation. FEBS Lett 359: 129-132.
18. Lu Z, Cyr DM, (1998) Protein folding activity of Hsp70 is modified differentially by the Hsp40 co-chaperones Sis1 and Ydj1. J Biol Chem 273: 27824-27830.
19. Fan CY, Lee S, Ren HY, Cyr DM, (2004) Exchangeable chaperone modules contribute to specification of type I and type II Hsp40 cellular function. Mol Biol Cell 15: 761-773.
20. Borges JC, Fischer H, Craievich AF, Ramos CHI, (2005) Low resolution structural study of two human HSP40 chaperones in solution- DjA1 from subfamily A and DjB4 from subfamily B have different quaternary structures. J Biol Chem 280: 13671-13681.
21. Ramos CHI, Oliveira CLP, Fan CY, Torriani IL, Cyr DM, (2008) Conserved Central Domains Control the Quaternary Structure of Type I and Type II Hsp40 Molecular Chaperones. J Mol Biol 383: 155-166.
22. Silva JC, Borges JC, Cyr DM, Ramos CHI, Torriani IL, (2011) Central domain deletions affect the SAXS solution structure and function of Yeast Hsp40 proteins Sis1 and Ydj1. BMC Struct Biol 11 40: 10.1186/1472-6807-11-40.
23. Schuck P, (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys J 78: 1606-1619.
24. Borges JC, Ramos CHI, (2011) Analysis of molecular targets of mycobacterium tuberculosis by analytical ultracentrifugation. Curr Med Chem 18: 1276-1285.
25. Tugarinov V, Kanelis V, Kay LE, (2006) Isotope labeling strategies for the study of high-molecular-weight proteins by solution NMR spectroscopy. Nat Protocols 1 749-754: 10.1038/nprot.2006.101.
26. Pervushin K, Wider G, Wüthrich K, (1998) Single Transition-to-single Transition Polarization Transfer (ST2-PT) in [15N,1H]-TROSY. J Biomol NMR 12: 345-348.
27. Kay L, Keifer P, Saarinen T, (1992) Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J Am Chem Soc 114: 10663-10665 doi:10.1021/ja00052a088.
28. Ramos CHI, Kay MS, Baldwin RL, (1999) Putative Interhelix Ion Pairs Involved in the Stability of Myoglobin. Biochemistry 38: 9783-9790 doi:10.1021/bi9828627.
29. Ramos CHI, Ferreira ST, (2005) Protein folding, misfolding and aggregation: Evolving concepts and conformational diseases. Protein Pept Lett 12: 213-222.
30. Laufen T, Mayer MP, Beisel C, Klostermeier D, Mogk A, et al. (1999) Mechanism of regulation of Hsp70 chaperones by DnaJ cochaperones. Proc Natl Acad Sci U S A 96: 5452-5457.
31. Pierpaoli EV, Sandmeier E, Schönfeld HJ, Christen P, (1998) Control of the DnaK Chaperone Cycle by Substoichiometric Concentrations of the Co-chaperones DnaJ and GrpE. J Biol Chem 273: 6643-6649.