Functional characterization of orchardgrass endoplasmic reticulum-resident Hsp90 (DgHsp90) as a chaperone and an ATPase

Hsp90 proteins are essential molecular chaperones regulating multiple cellular processes in distinct subcellular organelles. In this study, we report the functional characterization of a cDNA encoding endoplasmic reticulum (ER)-resident Hsp90 from orchardgrass (DgHsp90). DgHsp90 is a 2742bp cDNA wit...

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Veröffentlicht in:Plant physiology and biochemistry : PPB. - 1991. - 47(2009), 10 vom: 15. Okt., Seite 859-66
1. Verfasser: Cha, Joon-Yung (VerfasserIn)
Weitere Verfasser: Jung, Min Hee, Ermawati, Netty, Su'udi, Mukhamad, Rho, Gyu-Jin, Han, Chang-Deok, Lee, Kon Ho, Son, Daeyoung
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2009
Zugriff auf das übergeordnete Werk:Plant physiology and biochemistry : PPB
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Benzoquinones DNA, Complementary HSP90 Heat-Shock Proteins Lactams, Macrocyclic Molecular Chaperones Oxidants Plant Proteins Hydrogen Peroxide mehr... BBX060AN9V Adenosine Triphosphatases EC 3.6.1.- geldanamycin Z3K3VJ16KU
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245 1 0 |a Functional characterization of orchardgrass endoplasmic reticulum-resident Hsp90 (DgHsp90) as a chaperone and an ATPase 
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520 |a Hsp90 proteins are essential molecular chaperones regulating multiple cellular processes in distinct subcellular organelles. In this study, we report the functional characterization of a cDNA encoding endoplasmic reticulum (ER)-resident Hsp90 from orchardgrass (DgHsp90). DgHsp90 is a 2742bp cDNA with an open reading frame predicted to encode an 808 amino acid protein. DgHsp90 has a well conserved N-terminal ATPase domain and a C-terminal Hsp90 domain and ER-retention motif. Expression of DgHsp90 increased during heat stress at 35 degrees C or H(2)O(2) treatment. DgHsp90 also functions as a chaperone protein by preventing thermal aggregation of malate dehydrogenase (EC 1.1.1.37) and citrate synthase (EC 2.3.3.1). The intrinsic ATPase activity of DgHsp90 was inhibited by geldanamycin, an Hsp90 inhibitor, and the inhibition reduced the chaperone activity of DgHsp90. Yeast cells overexpressing DgHsp90 exhibited enhanced thermotolerance 
650 4 |a Journal Article 
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650 7 |a DNA, Complementary  |2 NLM 
650 7 |a HSP90 Heat-Shock Proteins  |2 NLM 
650 7 |a Lactams, Macrocyclic  |2 NLM 
650 7 |a Molecular Chaperones  |2 NLM 
650 7 |a Oxidants  |2 NLM 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a Hydrogen Peroxide  |2 NLM 
650 7 |a BBX060AN9V  |2 NLM 
650 7 |a Adenosine Triphosphatases  |2 NLM 
650 7 |a EC 3.6.1.-  |2 NLM 
650 7 |a geldanamycin  |2 NLM 
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700 1 |a Jung, Min Hee  |e verfasserin  |4 aut 
700 1 |a Ermawati, Netty  |e verfasserin  |4 aut 
700 1 |a Su'udi, Mukhamad  |e verfasserin  |4 aut 
700 1 |a Rho, Gyu-Jin  |e verfasserin  |4 aut 
700 1 |a Han, Chang-Deok  |e verfasserin  |4 aut 
700 1 |a Lee, Kon Ho  |e verfasserin  |4 aut 
700 1 |a Son, Daeyoung  |e verfasserin  |4 aut 
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