Expression of a conserved family of cytoplasmic low molecular weight heat shock proteins during heat stress and recovery

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 exp...

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Bibliographic Details
Published in:Plant physiology (Bethesda) 1991-08, Vol.96 (4), p.1038-1047
Main Authors: DeRocher, A.E. (University of Arizona, Tucson, AZ), Helm, K.W, Lauzon, L.M, Vierling, E
Format: Article
Language:English
Subjects:
AGOTAMIENTO POR EL CALOR
Amino acids
Antiserum
ARN MENSAJERO
ARN MESSAGER
Biological and medical sciences
Chloroplasts
Complementary DNA
COUP DE CHALEUR
EXPRESION GENICA
EXPRESSION DES GENES
Fundamental and applied biological sciences. Psychology
Gene expression
GENETICA
GENETIQUE
Heat shock proteins
Messenger RNA
Molecular and cellular biology
Molecular genetics
Peas
PESO MOLECULAR
PISUM SATIVUM
Plants
POIDS MOLECULAIRE
PROTEINAS
PROTEINE
RNA
SINTESIS DE PROTEINAS
Soybeans
SYNTHESE PROTEIQUE
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Summary: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
ISSN:0032-0889
1532-2548
DOI:10.1104/pp.96.4.1038