Heat-induced chaperone activity of serine/threonine protein phosphatase 5 enhances thermotolerance in Arabidopsis thaliana

© 2011 The Authors. New Phytologist © 2011 New Phytologist Trust.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1990. - 191(2011), 3 vom: 15. Aug., Seite 692-705
1. Verfasser: Park, Jin Ho (VerfasserIn)
Weitere Verfasser: Lee, Sun Yong, Kim, Woe Yeon, Jung, Young Jun, Chae, Ho Byoung, Jung, Hyun Suk, Kang, Chang Ho, Shin, Mi Rim, Kim, Sun Young, Su'udi, Mukhamad, Yun, Dae Jin, Lee, Kyun Oh, Kim, Min Gab, Lee, Sang Yeol
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2011
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Arabidopsis Proteins Molecular Chaperones Nuclear Proteins Recombinant Proteins Phosphoprotein Phosphatases EC 3.1.3.16 protein phosphatase 5
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245 1 0 |a Heat-induced chaperone activity of serine/threonine protein phosphatase 5 enhances thermotolerance in Arabidopsis thaliana 
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520 |a © 2011 The Authors. New Phytologist © 2011 New Phytologist Trust. 
520 |a • This study reports that Arabidopsis thaliana protein serine/threonine phosphatase 5 (AtPP5) plays a pivotal role in heat stress resistance. A high-molecular-weight (HMW) form of AtPP5 was isolated from heat-treated A. thaliana suspension cells. AtPP5 performs multiple functions, acting as a protein phosphatase, foldase chaperone, and holdase chaperone. The enzymatic activities of this versatile protein are closely associated with its oligomeric status, ranging from low oligomeric protein species to HMW complexes. • The phosphatase and foldase chaperone functions of AtPP5 are associated primarily with the low-molecular-weight (LMW) form, whereas the HMW form exhibits holdase chaperone activity. Transgenic over-expression of AtPP5 conferred enhanced heat shock resistance to wild-type A. thaliana and a T-DNA insertion knock-out mutant was defective in acquired thermotolerance. A recombinant phosphatase mutant (H290N) showed markedly increased holdase chaperone activity. • In addition, enhanced thermotolerance was observed in transgenic plants over-expressing H290N, which suggests that the holdase chaperone activity of AtPP5 is primarily responsible for AtPP5-mediated thermotolerance. • Collectively, the results from this study provide the first evidence that AtPP5 performs multiple enzymatic activities that are mediated by conformational changes induced by heat-shock stress 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 7 |a Arabidopsis Proteins  |2 NLM 
650 7 |a Molecular Chaperones  |2 NLM 
650 7 |a Nuclear Proteins  |2 NLM 
650 7 |a Recombinant Proteins  |2 NLM 
650 7 |a Phosphoprotein Phosphatases  |2 NLM 
650 7 |a EC 3.1.3.16  |2 NLM 
650 7 |a protein phosphatase 5  |2 NLM 
650 7 |a EC 3.1.3.16  |2 NLM 
700 1 |a Lee, Sun Yong  |e verfasserin  |4 aut 
700 1 |a Kim, Woe Yeon  |e verfasserin  |4 aut 
700 1 |a Jung, Young Jun  |e verfasserin  |4 aut 
700 1 |a Chae, Ho Byoung  |e verfasserin  |4 aut 
700 1 |a Jung, Hyun Suk  |e verfasserin  |4 aut 
700 1 |a Kang, Chang Ho  |e verfasserin  |4 aut 
700 1 |a Shin, Mi Rim  |e verfasserin  |4 aut 
700 1 |a Kim, Sun Young  |e verfasserin  |4 aut 
700 1 |a Su'udi, Mukhamad  |e verfasserin  |4 aut 
700 1 |a Yun, Dae Jin  |e verfasserin  |4 aut 
700 1 |a Lee, Kyun Oh  |e verfasserin  |4 aut 
700 1 |a Kim, Min Gab  |e verfasserin  |4 aut 
700 1 |a Lee, Sang Yeol  |e verfasserin  |4 aut 
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