期刊
FASEB JOURNAL
卷 29, 期 11, 页码 4424-4434出版社
FEDERATION AMER SOC EXP BIOL
DOI: 10.1096/fj.15-270140
关键词
heat shock; small GTPase; structural change
资金
- Cooperative Research Program for Agriculture Science and Technology Development
- Rural Development Administration [PJ007850]
- Basic Science Research Program, through the National Research Foundation, Ministry of Education, Science, and Technology (Seoul, South Korea) [2012R1A1A2044337]
- National Research Foundation of Korea [2012R1A1A2044337] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
Guanosine triphosphatases (GTPases) function as molecular switches in signal transduction pathways that enable cells to respond to extracellular stimuli. Saccharomyces cerevisiae yeast protein two 1 protein (Ypt1p) is a monomeric small GTPase that is essential for endoplasmic reticulum-to-Golgi trafficking. By size-exclusion chromatography, SDS-PAGE, and native PAGE, followed by immunoblot analysis with an anti-Ypt1p antibody, we found that Ypt1p structurally changed from low-molecular-weight (LMW) forms to high-molecular-weight (HMW) complexes after heat shock. Based on our results, Ypt1p exhibited dual functions both as a GTPase and a molecular chaperone, and furthermore, heat shock induced a functional switch from that of a GTPase to a molecular chaperone driven by the structural change from LMW to HMW forms. Subsequently, we found, by using a galactose-inducible expression system, that conditional overexpression of YPT1 in yeast cells enhanced the thermotolerance of cells by increasing the survival rate at 55 degrees C by similar to 60%, compared with the control cells expressing YPT1 in the wild-type level. Altogether, our results suggest that Ypt1p is involved in the cellular protection process under heat stress conditions. Also, these findings provide new insight into the in vivo roles of small GTP-binding proteins and have an impact on research and the investigation of human diseases.
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