Plant Physiology 96:1038-1047 (1991)
© 1991 American Society of Plant Biologists
Environmental and Stress Physiology
Expression of a Conserved Family of Cytoplasmic Low Molecular Weight Heat Shock Proteins during Heat Stress and Recovery 1
Amy E. DeRocher,
Kenneth W. Helm,
Lisa M. Lauzon and
Elizabeth Vierling
Department of Molecular and Cellular Biology, University of Arizona, Tucson, Arizona, 85721,
Department of Biochemistry, University of Arizona, Tucson, Arizona, 85721
Plants synthesize several families of low molecular weight (LMW) heat shock proteins (HSPs) in response to elevated temperatures. We have characterized two cDNAs, HSP18.1 and HSP17.9, that encode members of the class I family of LMW HSPs from pea (Pisum sativum). In addition, we investigated the expression of these HSPs at the mRNA and protein levels during heat stress and recovery. HSP18.1 and HSP17.9 are 82.1% identical at the amino acid level and are 80.8 to 92.9% identical to class I LMW HSPs of other angiosperms. Heat stress experiments were performed using intact seedlings subjected to a gradual temperature increase and held at a maximum temperature of 30 to 42 degrees Celsius for 4 hours. HSP18.1 and HSP17.9 mRNA levels peaked at the beginning of the maximum temperature period and declined rapidly after the stress period. Antiserum against a HSP18.1 fusion protein recognized both HSP18.1 and HSP17.9 but not members of other families of LMW HSPs. The accumulation of HSP18.1-immunodetected protein was proportional to the severity of the heat stress, and the protein had a half-life of 37.7 ± 8 hours. The long half-life of these proteins supports the hypothesis that they are involved in establishing thermotolerance.
1 Research supported by U.S. Department of Agriculture Competitive Research Grants Office grant 88-37264-3914, U.S. Department of Agriculture Southwest Consortium grant 88-34186-3340, and State of Arizona HATCH Funds.
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