Rice transglutaminase gene Identification, protein expression, functionality, light dependence and specific cell location

Rice transglutaminase gene : Identification, protein expression, functionality, light dependence and specific cell location

Published by Elsevier Ireland Ltd.

Détails bibliographiques
Publié dans:Plant science : an international journal of experimental plant biology. - 1985. - 205-206(2013) vom: 27. Mai, Seite 97-110
Auteur principal: Campos, N (Auteur)
Autres auteurs: Castañón, S, Urreta, I, Santos, M, Torné, J M
Format: Article en ligne
Langue:English
Publié: 2013
Accès à la collection:Plant science : an international journal of experimental plant biology
Sujets:Journal Article Research Support, Non-U.S. Gov't Antibodies Plant Proteins Recombinant Proteins Transglutaminases EC 2.3.2.13 Calcium SY7Q814VUP
Description
Résumé:Published by Elsevier Ireland Ltd.
Transglutaminases (TGases), that catalyze post-translational modification of proteins, are scarcely known in plants. As part of a project to characterize transglutaminase genes in new plant species, the identification and characterization of a TGase in rice is presented. Using differential primers, a cDNA (tgo) of 1767bp from genomic rice DNA amplification was obtained. The primers were designed from the rice DNA sequence relatively homologous to the gene encoding active maize chloroplast TGase. Amino acid sequence of the deduced rice TGase protein (TGO) indicated that it contains the enzyme catalytic triad (Cys-His-Asp), three repeats, myristoylation domains and a leucine zipper motif. The TGO recombinant protein was characterized, showing specific activity regulation, and indicating that tgo encoded for an authentic TGase. Substrate preference and Ca(2+) dependent activity were also detected. In the rice plant TGO protein was immunolocalized in the grana chloroplasts, in protein vesicles near them, and in the bulliform cells. Immunoblot analyses, tgo mRNA expression, and TGase activity indicated that TGO expression in rice was light dependent and regulated by the illumination period. This work increases significantly our plant TGase understanding. Its functional role in rice, which is a good model system for C3 plants, is discussed
Description:Date Completed 10.09.2013
Date Revised 30.09.2020
published: Print-Electronic
GENBANK: FR717829, FR717830
Citation Status MEDLINE
ISSN:1873-2259
DOI:10.1016/j.plantsci.2013.01.014