Proteins arising during the late stages of embryogenesis in Pisum sativum L

• Published in: Planta Vol. 184; no. 1; p. 14
• Main Authors: Barratt, D.H.P. (Bristol Univ. (United Kingdom). Dept. of Agricultural Sciences), Clark, J.A
• Format: Journal Article
• Language: English
• Published: Germany 01.04.1991
• Subjects: ABA; Abscisin; ACIDE ABSCISSIQUE; ACIDO ABSCISICO; BIOSINTESIS; BIOSYNTHESE; BIOSYNTHESIS; Entwicklungsstadium; Erbse; ETAPAS DE DESARROLLO DE LA PLANTA; GRAINE; PISUM SATIVUM; PLANT DEVELOPMENTAL STAGES; PROTEINAS; PROTEINE; PROTEINS; Proteinsynthese; Samenentwicklung; SEEDS; SEMILLA; STADE DE DEVELOPPEMENT VEGETAL
• ISSN: 0032-0935; 1432-2048
• DOI: 10.1007/BF00208230

Two abscisic acid (ABA)-responsive seed proteins, ABR17 and ABR18 (ABA-responsive 17000-Mr and 18000-Mr, respectively), previously found to be induced in cultured embryos of pea (Pisum sativum L.) are major components synthesised during normal seed desiccation. The ABR17 and ABR18 proteins showed different patterns of accumulation. The ABR18 protein was abundant in the testa during early seed development but in desiccating seed it was synthesised in the embryo, indicating spacial as well as temporal regulation of expression. The ABR18 protein was undetectable soon after germination but reappeared after adding ABA. The ABR17 protein was not detected in the testa but appeared in the embryo just prior to maximum fresh weight. The ABR17 protein continued to be synthesised during germination and was also present in non-stressed leaves. A high level of endogenous ABA or added ABA increased levels of translatable ABR17 mRNA. The ABR17 and ABR18 proteins were further characterised so as to help determine their structure and function. Neither protein appeared to contain a signal peptide but both proteins appeared to be glycosylated. The proteins had similar amino-acid compositions and limited Nterminal analysis showed 56% sequence identity. Neither protein had any significant N-terminal sequence homology to any of the late embryogenesis-abundant (LEA) proteins or dehydrins. Both proteins, however, show striking homology with a pea disease-resistance-response protein and the major birch pollen allergen, indicating that the ABR17 and ABR18 proteins may be members of a distinct group of stress-induced proteins.