Biochemical and immunohistochemical characterization of Mimosa annexin

• Published in: Planta 2004-09, Vol.219 (5), p.867-875
• Main Authors: Hoshino, D, Hayashi, A, Temmei, Y, Kanzawa, N, Tsuchiya, T
• Format: Article
• Language: English
• Subjects: actin; Actins; Amino Acid Sequence; amino acid sequences; annexin; Annexins; Annexins - isolation & purification; Annexins - metabolism; Biochemistry; Biological and medical sciences; Calcium; calcium-binding proteins; Cell membranes; Conserved Sequence; Enzymes; Fundamental and applied biological sciences. Psychology; Immunohistochemistry; Metabolism; Mimosa - metabolism; Mimosa - ultrastructure; Mimosa pudica; molecular sequence data; Nastic movement; Phospholipids; Plant cells; Plant physiology and development; plant proteins; Plant Proteins - metabolism; Plants; protein binding; Pulvini; pulvinus; tissue distribution
• ISSN: 0032-0935; 1432-2048
• DOI: 10.1007/s00425-004-1285-7

To characterize the biochemical properties of plant annexin, we isolated annexin from Mimosa pudica L. and analyzed the biochemical properties conserved between Mimosa annexin and animal annexins, e.g. the ability to bind phospholipid and F-actin in the presence of calcium. We show that Mimosa annexin is distributed in a wide variety of tissues. Immunoblot analysis also revealed that the amount of annexin is developmentally regulated. To identify novel functions of Mimosa annexin, we examined the pattern of distribution and the regulation of its expression in the pulvinus. The amount of annexin in the pulvinus increased at night and was sensitive to abscisic acid; however, there was no detectable induction of annexin by cold or mechanical stimulus. Annexin distribution in the cell periphery during the daytime was changed to a cytoplasmic distribution at night, indicating that Mimosa annexin may contribute to the nyctinastic movement in the pulvinus.