A low temperature induced apoplastic protein isolated from Arachis hypogaea

We describe the isolation, characterization and identification of an Arachis hypogaea cold shock protein (AHCSP33). AHCSP33 is secreted into the leaf apoplast during low temperature exposure. N-terminal sequence of AHCSP33 shows homology to Thaumatin-Like (TL) protein family (also called Group5 Path...

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Bibliographic Details
Published in:	Phytochemistry (Oxford) Vol. 49; no. 8; pp. 2207 - 2213
Main Authors:	Dave, Rajnish S, Mitra, Ranjit K
Format:	Journal Article
Language:	English
Published:	Amsterdam Elsevier Ltd 01-12-1998 Elsevier
Subjects:	Agricultural and forest climatology and meteorology. Irrigation. Drainage Agricultural and forest meteorology Agronomy. Soil science and plant productions Amino Acid Sequence apoplastic protein Arachis - chemistry Arachis hypogaea Biological and medical sciences Chromatography, Ion Exchange Climatic adaptation. Acclimatization cold induced protein Cold Temperature cryoprotective protein Electrophoresis, Polyacrylamide Gel Fabaceae Fundamental and applied biological sciences. Psychology General agronomy. Plant production groundnut Heat-Shock Proteins - biosynthesis Heat-Shock Proteins - chemistry Heat-Shock Proteins - isolation & purification Molecular Sequence Data Physical agents Plant physiology and development Sequence Homology, Amino Acid thaumatin-like proteins Vegetative apparatus, growth and morphogenesis. Senescence groundnut cold induced protein cryoprotective protein Arachis hypogaea apoplastic protein thaumatin-like proteins Fabaceae Thaumatin Cold Homology Plant leaf Apoplast Pathogenesis related protein Oil plant(vegetal) Biological activity Characterization Leguminosae Disulfide bond Protein synthesis Dicotyledones Angiospermae Heat shock protein N terminal-Sequence Spermatophyta Cryoprotective agent Antifreeze protein Low temperature
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Summary:	We describe the isolation, characterization and identification of an Arachis hypogaea cold shock protein (AHCSP33). AHCSP33 is secreted into the leaf apoplast during low temperature exposure. N-terminal sequence of AHCSP33 shows homology to Thaumatin-Like (TL) protein family (also called Group5 Pathogenesis-related (PR) proteins). AHCSP33 shows strongest homology (55%) at the N-terminus with the Rye TL protein ( M r 25 k) which is an apoplastic protein and has antifreeze activity. Like several TL proteins, AHCSP33 is also targeted to the apoplast and persists for several days after low temperature treatment, although at reduced levels. AHCSP33 possesses intrachain disulfide bonds which is a well conserved feature of TL proteins. AHCSP33 might be involved in cryoprotecting proteins as it was shown to prevent freeze-induced denaturation of l-lactate dehydrogenase (LDH). Several features of AHCSP33 are consistent with its role in cryoprotection. It is a hydrophilic protein and is boiling stable. Hydrophilic amino acids constitute 80.4 mol%. Asp/Asn and Glu/Gln together constitute 20.8 mol%. AHCSP33 is glycosylated and exists as an oligomer in its native state.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0031-9422 1873-3700
DOI:	10.1016/S0031-9422(98)00372-0