期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 20, 期 1, 页码 -出版社
MDPI
DOI: 10.3390/ijms20010132
关键词
small GTPase; heat-shock; molecular chaperone; structural change; functional switch
资金
- NG-BioGreen 21 Program (SSAC) [PJ01317301, PJ01334001]
- Basic Science Research Program through the National Research Foundation - MOEST, Korea [2016R1D1A1B01016551]
- RDA
- National Research Foundation of Korea [2016R1D1A1B01016551] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
In our previous study, we found that Ypt1p, a Rab family small GTPase protein, exhibits a stress-driven structural and functional switch from a GTPase to a molecular chaperone, and mediates thermo tolerance in Saccharomyces cerevisiae. In the current study, we focused on the temperature-sensitive ypt1-G80D mutant, and found that the mutant cells are highly sensitive to heat-shock, due to a deficiency in the chaperone function of Ypt1p(G80D). This defect results from an inability of the protein to form high molecular weight polymers, even though it retains almost normal GTPase function. The heat-stress sensitivity of ypt1-G80D cells was partially recovered by treatment with 4-phenylbutyric acid, a chemical chaperone. These findings indicate that loss of the chaperone function of Ypt1p(G80D) underlies the heat sensitivity of ypt1-G80D cells. We also compared the proteomes of YPT1 (wild-type) and ypt1-G80D cells to investigate Ypt1p-controlled proteins under heat-stress conditions. Our findings suggest that Ypt1p controls an abundance of proteins involved in metabolism, protein synthesis, cellular energy generation, stress response, and DNA regulation. Finally, we suggest that Ypt1p essentially regulates fundamental cellular processes under heat-stress conditions by acting as a molecular chaperone.
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