The molecular structure and evolutionary relationships of a 16.9 kDa heat shock protein from Norway spruce [Picea abies (L.) Karst.]

Based on an elicitor-induced cDNA library from Picea abies (L.) Karst. (Norway spruce), clone pPA0010 encoding a small heat shock protein of 16.91 kDa molecular weight was identified. Comparison of the deduced amino acid sequence with gene bank data revealed significant similarities to cytosolic cla...

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Published inForest Genetics (Zvolen) Vol. 4; no. 3
Main Authors Schubert, R, Muller-Starck, G. (Ludwig Maximilians Univ. of Munich, Freising (Germany). Faculty of Forest Sciences, Section of Forest Genetics), Sandermann, H, Ernst, D, Hager, K.P
Format Journal Article
LanguageEnglish
Published 1997
Subjects
ESTRES TERMICO
EVOLUCION
EVOLUTION
PICEA ABIES
PROTEINAS
PROTEINE
PROTEINS
STRESS THERMIQUE
THERMAL STRESS
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Summary:Based on an elicitor-induced cDNA library from Picea abies (L.) Karst. (Norway spruce), clone pPA0010 encoding a small heat shock protein of 16.91 kDa molecular weight was identified. Comparison of the deduced amino acid sequence with gene bank data revealed significant similarities to cytosolic class II small heat shock proteins. Evolutionary relationships to small heat shock proteins from Picea glauca and Pseudotsuga menziesii and to those from angiospermous species were analysed using distance matrix- and parsimony-methods, respectively. The different classes of small heat shock proteins appear to have already existed in the last common ancestor of extant seed plants, and further diversification has occurred within class II small heat shock proteins from Picea. Phosphorylation motifs for serine protein kinases were detected in the heat shock domains of Picea small heat shock proteins
Bibliography:F30
1998000639
ISSN:1335-048X