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 2742 bp cDNA w...

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Bibliographic Details
Published in:Plant physiology and biochemistry 2009-10, Vol.47 (10), p.859-866
Main Authors: Cha, Joon-Yung, Jung, Min Hee, Ermawati, Netty, Su'udi, Mukhamad, Rho, Gyu-Jin, Han, Chang-deok, Lee, Kon Ho, Son, Daeyoung
Format: Article
Language:English
Subjects:
Adaptation, Physiological
Adenosine Triphosphatases - genetics
Adenosine Triphosphatases - metabolism
Amino Acid Sequence
ATPase
Base Sequence
Benzoquinones - pharmacology
Biological and medical sciences
Blotting, Northern
Chaperone
Dactylis - genetics
Dactylis - metabolism
DNA, Complementary - chemistry
DNA, Complementary - genetics
Endoplasmic reticulum
Endoplasmic Reticulum - metabolism
Fundamental and applied biological sciences. Psychology
Gene Expression Profiling
Gene Expression Regulation, Plant - drug effects
Heat shock protein 90
Hot Temperature
HSP90 Heat-Shock Proteins - classification
HSP90 Heat-Shock Proteins - genetics
HSP90 Heat-Shock Proteins - metabolism
Hydrogen Peroxide - pharmacology
Lactams, Macrocyclic - pharmacology
Molecular Chaperones - genetics
Molecular Chaperones - metabolism
Molecular Sequence Data
Orchardgrass ( Dactylis glomerata L.)
Oxidants - pharmacology
Phylogeny
Plant physiology and development
Plant Proteins - classification
Plant Proteins - genetics
Plant Proteins - metabolism
Sequence Analysis, DNA
Thermotolerance
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Summary: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 2742 bp 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 °C or H 2O 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.
ISSN:0981-9428
1873-2690
DOI:10.1016/j.plaphy.2009.06.008