dc.contributor.author | Tutar, Y. | |
dc.contributor.author | Coskun, K. A. | |
dc.contributor.author | Tutar, L. | |
dc.date.accessioned | 2019-07-27T12:10:23Z | |
dc.date.accessioned | 2019-07-28T09:59:53Z | |
dc.date.available | 2019-07-27T12:10:23Z | |
dc.date.available | 2019-07-28T09:59:53Z | |
dc.date.issued | 2013 | |
dc.identifier.issn | 0006-2979 | |
dc.identifier.uri | https://dx.doi.org/10.1134/S0006297913050118 | |
dc.identifier.uri | https://hdl.handle.net/20.500.12418/8717 | |
dc.description | WOS: 000319219800011 | en_US |
dc.description | PubMed ID: 23848155 | en_US |
dc.description.abstract | Two fish species, Cyprinion macrostomus macrostomus and Garra rufa obtuse, tolerate adverse conditions in the Kangal hot springs and cope with multiple stressors such as food deprivation, extreme temperature, toxins, protein degradation, hypoxia, and microbial damage. These fish have evolved strategies to counteract the stressors including the induction of heat shock proteins (Hsps). Hsps play an essential role in maintaining cellular homeostasis, and one of the key proteins in the mechanism is Hsp70. Hsp70 itself is exposed to the same stressors as all other proteins, and, hence, the stability of Hsp70 was investigated. For this purpose, Hsp70 ATPase activity was determined at different urea concentrations. It was found that the protein maintains considerable ATP hydrolysis activity at higher denaturant conditions. Temperature effects on the substrate peptide binding showed that Hsp70s bind prominently at elevated temperatures. Furthermore, temperature effects on Hsp70 aggregation indicated that the presence of nucleotides decreases the aggregation process. The present work has determined the stability and activity of cmHsp70 and grHsp70 themselves under extreme conditions. The stability of the Hsp70 proteins maintains substrate proteins in the native state, which may aid in the adaptation of the fish species to the hot spring environment. | en_US |
dc.description.sponsorship | Turkish National Academy of Sciences [TUBA GEBIP 2008-29] | en_US |
dc.description.sponsorship | This work was funded partly by the CUBAP (F 253) project and through a seed grant from the Turkish National Academy of Sciences (TUBA GEBIP 2008-29). | en_US |
dc.language.iso | eng | en_US |
dc.publisher | MAIK NAUKA/INTERPERIODICA/SPRINGER | en_US |
dc.relation.isversionof | 10.1134/S0006297913050118 | en_US |
dc.rights | info:eu-repo/semantics/closedAccess | en_US |
dc.subject | Hsp70 | en_US |
dc.subject | stability | en_US |
dc.subject | aggregation | en_US |
dc.title | Hsp70 from Cyprinion macrostomus macrostomus and Garra rufa obtuse: Stability and stability-dependent activity | en_US |
dc.type | article | en_US |
dc.relation.journal | BIOCHEMISTRY-MOSCOW | en_US |
dc.contributor.department | [Tutar, Y.] Cumhuriyet Univ, Fac Pharmacol, Dept Biochem, TR-58140 Sivas, Turkey -- [Tutar, Y.] Cumhuriyet Univ, CUTFAM Res Ctr, Fac Med, TR-58140 Sivas, Turkey -- [Coskun, K. A.] Cumhuriyet Univ, Dept Parasitol, Fac Med, TR-58140 Sivas, Turkey -- [Tutar, L.] Kahramanmaras Sutcu Imam Univ, Dept Biol, Fac Sci & Letters, TR-46100 Kahramanmaras, Turkey | en_US |
dc.identifier.volume | 78 | en_US |
dc.identifier.issue | 5 | en_US |
dc.identifier.endpage | 535 | en_US |
dc.identifier.startpage | 531 | en_US |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | en_US |