Jp. Galaud et al., OSMOTIC-STRESS ACTIVATED EXPRESSION OF AN ARABIDOPSIS PLASMA MEMBRANE-ASSOCIATED PROTEIN - SEQUENCE AND PREDICTED SECONDARY STRUCTURE, Biochimica et biophysica acta. Protein structure and molecular enzymology, 1341(1), 1997, pp. 79-86
A cDNA clone At.MAMI (Arabidopsis thaliana membrane-associated mannito
l-induced) was isolated from an Arabidopsis cDNA expression library by
immunoselection. The cDNA was full-length (1.18 kb) with an open read
ing frame of 798 nucleotides encoding a 265 amino acid protein. The se
quence of At.MAMI did not show any significant identity with other gen
es, as well as the deduced amino acid sequence with other proteins. Ho
wever, prediction methods for the secondary structure of MAMI-30, toge
ther with homologous domains revealed some identity with VAP-33, a pro
tein involved in membrane trafficking in neuronal tissues. In contrast
to VAP-33, MAMI-30 did not exhibit a transmembrane domain, but positi
vely charged loop regions could be involved in membrane anchoring. Ind
eed, MAMI-30 was immunodetected in purified plasma membrane from Arabi
dopsis cells. The gene was responsive to low turgor in Arabidopsis and
its expression regulated developmentally. In addition, reduction of t
urgor caused a higher accumulation of mRNAs. (C) 1997 Elsevier Science
B.V.