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Immunolocalization of a novel annexin‐like protein encoded by a stress and abscisic acid responsive gene in alfalfa
Author(s) -
Kovács Izabella,
Ayaydin Ferhan,
Oberschall Attila,
Ipacs Ildikó,
Bottka Sándor,
Pongor Sándor,
Dudits Dénes,
Tóth Éva Csordás
Publication year - 1998
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1046/j.1365-313x.1998.00194.x
Subject(s) - abscisic acid , biology , peptide sequence , gene , complementary dna , amino acid , signal peptide , microbiology and biotechnology , biochemistry , gene expression , messenger rna
Summary We report here on the isolation and characterization of a full‐length cDNA clone from alfalfa termed AnnMs2 encoding a 333 amino acid long polypeptide that shows 32–37% sequence identity with both mammalian and plant annexins, and has four tandem repeats. While other plant annexins exhibit a high level of sequence similarity to each other (up to 77% identity at amino acid level), AnnMs2 appears to be a distinct type of plant annexins. All the four endonexin folds contain the conserved eukaryotic motif within this alfalfa protein, but this element is considerably different in the second repeat. The AnnMs2 gene is expressed in various tissues of alfalfa with elevated mRNA accumulation in root and flower. This gene is activated in cells or tissues exposed to osmotic stress, abscisic acid (ABA) or water deficiency. The recombinant AnnMs2 protein is able to bind to phospholipid in the presence of Ca 2+ . Indirect immunofluorescence studies using affinity purified rabbit anti‐AnnMs2 peptide antibody show mainly nucleolar localization, but the protein sequence lacks the usual nuclear localization signal. The potential role of this novel annexin‐like protein in the basic and stress‐induced cellular functions is discussed.