A low temperature induced apoplastic protein isolated from Arachis hypogaea

• 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
• ISSN: 0031-9422; 1873-3700
• DOI: 10.1016/S0031-9422(98)00372-0

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.