A novel cDNA clone osr40c1, encoding a environment and belongs to a no
vel plant protein family that most probably has structural functions.
abscisic acid (ABA)-responsive 40-kDa protein previously associated wi
th salt tolerance (Moons et al. '1995' Plant Physiol 107: 177-186), wa
s isolated from roots of rice seedlings (Oryza sativa L.). Exogenously
applied ABA and salt shock induced a marked increase of the asr40c1 t
ranscript level in roots of seedlings whereas constant osr40c1 mRNA le
vels were found in the shoot. The root-specific salinity-induced osr40
c1 mRNA accumulation was rapid and gradually declined upon prolonged s
alt shock. Plant growth regulators, signalling the wounding and the pa
thogen response, did not enhance osr40c1 expression, indicating a salt
- and osmotic-stress-specific response. The encoded OSR40c1 protein wa
s found to be hydrophilic, rich in histidine residues (6%) constitutin
g putative metal-binding domains, and to consist of a duplicated domai
n of 151 amino acids (75% identical), that can form amphiphilic a-heli
cal structures. The gene osr40c1 belongs to a multigene family. Two os
r40 genes were isolated, osr40g2 and osr40g3, tandemly arranged in an
8-kb region of the rice genome. Antisera raised against a conserved OS
R40 peptide recognized different OSR40 proteins that accumulated in ro
ots upon exposure to salt stress. The OSR40 protein family included 29
-kDa proteins and two 40-kDa proteins, the latter most probably corres
ponding to OSR40c1 and OSR40g2 with duplicated domain structures. The
osr40g3 transcript encoded a single copy of the OSR40 domain and exhib
ited a shoot-specific expression. Results indicate that OSR40c1 plays
a role in the adaptative response of roots to an hyper-osmotic environ
ment and belongs to a novel plant protein family that most probably ha
s structural functions.