Heat shock protein 70 purification and characterization from Cyprinion macrastomus macrastomus and Garra rufa obtusa

Journal of Thermal Biology

Volumn 37, Issue 1, 2012, Pages 95-99

  Tutar, Yusuf ^a   Okan, Şule ^a  

^a CUMHURIYET UNIVERSITY   (Turkey)

Author keywords

ATPase; Hsp70; Luciferase; Protein aggregation; Protein folding

Indexed keywords

ADENOSINE TRIPHOSPHATASE; HEAT SHOCK PROTEIN 70;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CELLULAR DISTRIBUTION; CONTROLLED STUDY; CYPRINION MACROSTOMUS MACROSTOMUS; ENVIRONMENTAL TEMPERATURE; FISH; FOOD DEPRIVATION; GARRA RUFA OBTUSA; HEAT STRESS; HYPOXIA; IN VITRO STUDY; NONHUMAN; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PURIFICATION; SPECIES COMPARISON; TEMPERATURE MEASUREMENT; THERMAL SPRING; THERMOSTABILITY; TURKEY (REPUBLIC); WATER TEMPERATURE;

CYPRINIDAE; CYPRINION; CYPRINION MACROSTOMUS; GARRA RUFA;

EID: 84155164699     PISSN: 03064565     EISSN: 18790992     Source Type: Journal    
DOI: 10.1016/j.jtherbio.2011.11.002     Document Type: Article

References (30)

1. Al-Habib O.A.M., Al-Habib W.M.S. Acclimation to temperature and death at high changing lethal temperatures in Cyprinion macrostomus (Heckel). J. Therm. Biol. 1979, 4:75-77.
2. Bukau B., Weissman J., Horwich A. Molecular chaperones and protein quality control. Cell 2006, 125:443-451.
3. Chen Q., Wang.Z., Xiong Y., Xue W., Kao X., Gao Y., Muhammad N, Song D. Selenium increases expression of Hsp70 and antioxidant enzymes to lessen oxidative damage in fincoal-type fluorosis. J. Toxicol. Sci. 2009, 34:399-405.
4. Chernoff Y.O., Lindquist S.L., Ono B., Inge-Vechtomov S.G., Liebman S.W. Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [PSI+]. Science 1995, 268:880-884.
5. Craig E.A., Gross C.A. Is Hsp70 the cellular thermometer?. Trends Biochem. Sci. 1991, 16:135-140.
6. Demir N. Ihtiology 2009, Nobel Press, Ankara, Turkey. first ed.
7. Fan C.Y., Lee S., Cyr D.M. Mechanisms for regulation of Hsp70 function by Hsp40. Cell Stress Chaperones 2003, 8:309-316.
8. Fan C.Y., Lee S., Ren H.Y., Cyr D.M. Exchangeable chaperone modules contribute to specification of type I and type II Hsp40 cellular function. Mol. Biol. Cell 2004, 15:761-773.
9. Fung K.L., Hilgenberg L., Wang N.M., Chirico W.J. Conformations of the nucleotide and polypeptide binding domains of a cytosolic Hsp70 molecular chaperone are coupled. J. Biol. Chem. 1996, 271:21559-21565.
10. Glover J.R., Lindquist S. Hsp104, Hsp70, and Hsp40, a novel chaperone system that rescues previously aggregated proteins. Cell 1998, 94:73-83.
11. Gözükara, E.S., Çavas, T., 2001. Cytogenetic analysis of Garra rufa obtusa (Heckel, 1843) from eastern Mediterranean river systems. In: Proceedings of the Third European Cytogenetics Conference Annales de Génétique, Supplement 1, pp. 43-44.
12. Harrison C.J., Hayer-Hartl M., Di Liberto M., Hartl F., Kuriyan J. Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science 1997, 276:431-435.
13. Haslbeck M., Buchner J. Chaperone function of sHsps. Prog. Mol. Subcell. Biol. 2002, 28:37-59.
14. Haslbeck M. sHsps and their role in the chaperone network. Cell. Mol. Life Sci. 2002, 59:1649-1657.
15. Jones G.W, Masison D.C. Saccharomyces cerevisiae Hsp70 mutations affect [PSI+] prion propagation and cell growth differently and implicate Hsp40 and tetratricopeptide repeat cochaperones in impairment of [PSI+]. Genetics 2003, 163:495-506.
16. Kabani M., Beckerich J.M., Brodsky J.L. Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p. Mol. Cell. Biol. 2002, 22:4677-4689.
17. Kuru M. The freshwater fish of south-eastern Turkey-2 (Euphrates-Tigris Systeme). Hacettepe Bull. Nat. Sci. Eng. 1979, 7:105-114.
18. Lu Z., Cyr D.M. Protein folding activity of Hsp70 is modified differentially by the Hsp40 co-chaperones Sis1 and Ydj1. J. Biol. Chem. 1998, 23:27824-27830.
19. McCarty J.S., Buchberger A., Reinstein J., Bukau B. The role of ATP in the functional cycle of the DnaK chaperone system. J. Mol. Biol. 1995, 249:126-137.
20. Özer Z., Akpinar M.A., Akçay A., Erdem Ü., Güler R., Yanikoĝlu A., Ergenoĝlu B., Ünal Ş., Savaşçi Ş. Kangal balikli kaplicanin bazi kimyasal ve biyolojik özelliklerinin araştiriilmasi. CÜ Fen Bilimleri Derg. 1987, 5:1-34.
21. Place S.P., Hofmann G.E. Temperature interactions of the molecular chaperone Hsc70 from the eurythermal marine goby Gillichthys mirabilis. J. Exp. Biol. 2001, 204:2675-2782.
22. Russell R., Jordan R., McMacken R. Kinetic characterization of the ATPase cycle of the DnaK molecular chaperone. Biochemistry 1998, 13:596-607.
23. Shorter J.S., Lindquist S. Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions. EMBO J. 2008, 27:2712-2714.
24. Song Y., Wu Y.X., Jung G., Tutar Y., Eisenberg E., Greene L.E., Masison D.C. Role for Hsp70 chaperone in Saccharomyces cerevisiae prion seed replication. Eukaryotic Cell 2005, 4:289-297.
25. Summers D.W, Douglas P.M, Ramos C.H, Cyr D.M. Polypeptide transfer from Hsp40 to Hsp70 molecular chaperones. Trends Biochem. Sci. 2009, 34:230-233.
26. Tutar Y., Song Y., Masison D.C. Primate chaperones Hsc70 (constitutive) and Hsp70 (induced) differ functionally in supporting growth and prion propagation in Saccharomyces cerevisiae. Genetics 2006, 172:851-861.
27. Tutar Y. Prelude, cellular mechanics. Protein Pept. Lett. 2009, 16:570.
28. Tutar L., Tutar Y. Heat shock proteins, an overview. Curr. Pharm. Biotechnol. 2010, 11:216-222.
29. Undar L., Akpinar M.A., Yanikoĝlu A. Doctor fish and psoriasis. The Lancet 1990, 335:470-471.
30. Weibezahn J., Schlieker C., Tessarz P., Mogk A., Bukau B. Novel insights into the mechanism of chaperone-assisted protein disaggregation. Biol. Chem. 2005, 386:739-744.