Effect of temperature on the role of Hsp104 and trehalose in barotolerance of Saccharomyces cerevisiae
We have studied the effect of temperature on the contribution of Hsp104 and trehalose to barotolerance using mutants deficient in Hsp104 and trehalose synthesis. When compared with a corresponding wild type strain, mutants of Hsp104 did not show temperature dependent barotolerance when the incubatio...
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Veröffentlicht in: | FEBS letters 1997-10, Vol.416 (1), p.1-5 |
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description | We have studied the effect of temperature on the contribution of Hsp104 and trehalose to barotolerance using mutants deficient in Hsp104 and trehalose synthesis. When compared with a corresponding wild type strain, mutants of Hsp104 did not show temperature dependent barotolerance when the incubation temperature during the hydrostatic pressure treatment was increased. However, a mutant deficient in trehalose synthesis showed features similar to a wild type strain. Furthermore, the Hsp104 level was low in the insoluble fraction of the wild type strain after pressure treatment at 35°C but not at 4°C, and the protein profiles in the insoluble fraction were different between 35°C and 4°C. In contrast to the Hsp104 deficient mutants, the protein profile of the wild type after pressure treatment at 35°C favors the role of Hsp104 as a disaggregator of proteins during hydrostatic pressure stress. These results suggest that the role of Hsp104 in barotolerance is temperature dependent in contrast to trehalose. |
doi_str_mv | 10.1016/S0014-5793(97)01141-1 |
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When compared with a corresponding wild type strain, mutants of Hsp104 did not show temperature dependent barotolerance when the incubation temperature during the hydrostatic pressure treatment was increased. However, a mutant deficient in trehalose synthesis showed features similar to a wild type strain. Furthermore, the Hsp104 level was low in the insoluble fraction of the wild type strain after pressure treatment at 35°C but not at 4°C, and the protein profiles in the insoluble fraction were different between 35°C and 4°C. In contrast to the Hsp104 deficient mutants, the protein profile of the wild type after pressure treatment at 35°C favors the role of Hsp104 as a disaggregator of proteins during hydrostatic pressure stress. 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When compared with a corresponding wild type strain, mutants of Hsp104 did not show temperature dependent barotolerance when the incubation temperature during the hydrostatic pressure treatment was increased. However, a mutant deficient in trehalose synthesis showed features similar to a wild type strain. Furthermore, the Hsp104 level was low in the insoluble fraction of the wild type strain after pressure treatment at 35°C but not at 4°C, and the protein profiles in the insoluble fraction were different between 35°C and 4°C. In contrast to the Hsp104 deficient mutants, the protein profile of the wild type after pressure treatment at 35°C favors the role of Hsp104 as a disaggregator of proteins during hydrostatic pressure stress. These results suggest that the role of Hsp104 in barotolerance is temperature dependent in contrast to trehalose.</description><subject>Adaptation, Physiological - physiology</subject><subject>Barotolerance</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Heat-Shock Proteins - physiology</subject><subject>Hsp104</subject><subject>Hydrostatic pressure</subject><subject>Pressure</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - physiology</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Temperature</subject><subject>Trehalose</subject><subject>Trehalose - physiology</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNUU1r3DAQFaEl2ab5CQGdSntwq5FsyTqVNmyyhUAPac9Clkesgj-2kjdh_31l75JrchKa9zHDe4RcA_sKDOS3B8agLCqlxWetvjCAEgo4IyuolShEKet3ZPVCuSAfUnpk-V-DPifnWkjNOVsRv_Ye3URHTyfsdxjttI9Ix4FOW6Rx7HCGNmkHrKR2aOkUcWu7MSENA21sHKfMiXZwC_HBOrfNw_7gMFGHEZ9CChY_kvfedgmvTu8l-Xu7_nOzKe5_3_26-XFfuIpzKGTTKNkKoVuJEnnFvPXK8kpZVoq2lkx6rwGgFrwE4bTAsmwkMpQgtRdaXJJPR99dHP_tMU2mD8lh19kBx30ySmcdfwMRJBcgqzoTqyPRxTGliN7sYuhtPBhgZi7CLEWYOWWjlVmKMJB116cF-6bH9kV1Sj7jmyP-HDo8vM3U3K5_8gWZAa2W8bzq-9EKc7JPAaNJLmBupA0xd2vaMbxy7H_qIKqg</recordid><startdate>19971013</startdate><enddate>19971013</enddate><creator>Iwahashi, Hitoshi</creator><creator>Obuchi, Kaoru</creator><creator>Fujii, Shinsuke</creator><creator>Komatsu, Yasuhiko</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>M7N</scope><scope>7X8</scope></search><sort><creationdate>19971013</creationdate><title>Effect of temperature on the role of Hsp104 and trehalose in barotolerance of Saccharomyces cerevisiae</title><author>Iwahashi, Hitoshi ; Obuchi, Kaoru ; Fujii, Shinsuke ; Komatsu, Yasuhiko</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5221-6bb76d339d6e6e250faf7a257a043d8606ff9111832413c93e44b6e0e6169f393</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Adaptation, Physiological - physiology</topic><topic>Barotolerance</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Heat-Shock Proteins - physiology</topic><topic>Hsp104</topic><topic>Hydrostatic pressure</topic><topic>Pressure</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - physiology</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>Temperature</topic><topic>Trehalose</topic><topic>Trehalose - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Iwahashi, Hitoshi</creatorcontrib><creatorcontrib>Obuchi, Kaoru</creatorcontrib><creatorcontrib>Fujii, Shinsuke</creatorcontrib><creatorcontrib>Komatsu, Yasuhiko</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Iwahashi, Hitoshi</au><au>Obuchi, Kaoru</au><au>Fujii, Shinsuke</au><au>Komatsu, Yasuhiko</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effect of temperature on the role of Hsp104 and trehalose in barotolerance of Saccharomyces cerevisiae</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1997-10-13</date><risdate>1997</risdate><volume>416</volume><issue>1</issue><spage>1</spage><epage>5</epage><pages>1-5</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>We have studied the effect of temperature on the contribution of Hsp104 and trehalose to barotolerance using mutants deficient in Hsp104 and trehalose synthesis. When compared with a corresponding wild type strain, mutants of Hsp104 did not show temperature dependent barotolerance when the incubation temperature during the hydrostatic pressure treatment was increased. However, a mutant deficient in trehalose synthesis showed features similar to a wild type strain. Furthermore, the Hsp104 level was low in the insoluble fraction of the wild type strain after pressure treatment at 35°C but not at 4°C, and the protein profiles in the insoluble fraction were different between 35°C and 4°C. In contrast to the Hsp104 deficient mutants, the protein profile of the wild type after pressure treatment at 35°C favors the role of Hsp104 as a disaggregator of proteins during hydrostatic pressure stress. These results suggest that the role of Hsp104 in barotolerance is temperature dependent in contrast to trehalose.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>9369220</pmid><doi>10.1016/S0014-5793(97)01141-1</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Adaptation, Physiological - physiology Barotolerance Electrophoresis, Gel, Two-Dimensional Heat-Shock Proteins - physiology Hsp104 Hydrostatic pressure Pressure Saccharomyces cerevisiae Saccharomyces cerevisiae - physiology Saccharomyces cerevisiae Proteins Temperature Trehalose Trehalose - physiology |
title | Effect of temperature on the role of Hsp104 and trehalose in barotolerance of Saccharomyces cerevisiae |
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