P. Coutosthevenot et al., 4 9-KDA PROTEINS EXCRETED BY SOMATIC EMBRYOS OF GRAPEVINE ARE ISOFORMS OF LIPID-TRANSFER PROTEINS, European journal of biochemistry, 217(3), 1993, pp. 885-889
Four 9-kDa small extracellular proteins produced by embryogenic cultur
es in the absence of auxin have been purified from the extracellular m
edium of grapevine somatic embryo cultures through cation-exchange chr
omatography and hydrophobic-interaction chromatography. The partial am
ino-acid sequences reflect high similarities between the four proteins
as well as with the sequences established for carrot, spinach, millet
and maize nonspecific lipid-transfer proteins. All these sequences sh
ow conservation of three cysteines at positions 4, 14 and 30-32, as we
ll as glycine, valine, tyrosine and lysine residues at positions 5, 7,
17 and 37, respectively. In-vitro lipid-transfer assays reveal that t
he four proteins catalyze the transfer of phosphatidylcholine from lip
osomes towards motochondria with an efficiency similar or higher than
that of a purified maize lipid-transfer protein.