Int. J. Dev. Biol. 45: S63 - S64 (2001)

Vol 45, Issue S1

Characterization of seed storage proteins and their synthesis during seed development in Olea europaea

Published: 1 June 2001

W Wang, J De-Dios-Alche, AJ Castro, MI Rodriguez-Garcia

CSIC, Estac Expt Zaidin, Dept Bioquim Biol Celular & Mol Plantas, E-18008 Granada, Spain

Abstract

SDS-PAGE analysis showed that seed storage proteins (SSPs) in olive mainly consisted of two hydrogen-bonded subunits, Solea I (41 kDa) and Solea II (47.5 kDa). When reduced, Solea I and II yielded 3 and 2 disulfide-bonded polypeptides, respectively. N-terminal sequencing confirmed that both Solea I and II shared a high similarity with II S proteins. Additionally, time-course of protein synthesis in olive seeds was investigated from 25 days after anthesis (DAA) until seed ripening. Before 105 DAA, young seeds contained only trace amounts of detectable proteins. Only from 105 DAA onwards, seed proteins began to be massively synthesized. Seeds of 105 DAA and more exhibited no significant difference in protein profiles with mature seeds, especially in terms of Solea I and II.

Keywords

Sequence, subunit