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JXB Advance Access published online on November 1, 2005
Journal of Experimental Botany, doi:10.1093/jxb/eri313
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© The Author [2005]. Published by Oxford University Press [on behalf of the Society for Experimental Biology]. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org
Received July 27, 2005
Accepted September 1, 2005

RESEARCH PAPER

A multifunctional bicupin serves as precursor for a chromosomal protein of Pisum sativum seeds

Josefa Castillo 1, Ainhoa Genovés 2, Luis Franco 3*, and M. Isabel Rodrigo 3

1 Department of Biochemistry and Molecular Biology, University of Valencia, E-46100, Burjassot, Valencia, Spain; Present address: División de Hepatología y Terapia Génica, CIMA, Departamento de Medicina Interna, Universidad de Navarra, Spain
2 Department of Biochemistry and Molecular Biology, University of Valencia, E-46100, Burjassot, Valencia, Spain; Present address: Instituto de Biologia Molecular y Celular de Plantas, CSIC, Valencia, Spain
3 Department of Biochemistry and Molecular Biology, University of Valencia, E-46100, Burjassot, Valencia, Spain

* To whom correspondence should be addressed.
Luis Franco, E-mail: luis.franco{at}uv.es


  Abstract

The fact that the psp54 gene codes for p16, a seed chromatin protein of Pisum sativum, has been described previously. In the present paper it is shown that p54, the p16 precursor, also exists as a free polypeptide in pea and that it also yields p38, a second polypeptide from the N-terminal region of p54, which is co-localized at a subcellular level with p16. By using antibodies against pea p16 and p38, it was found that these proteins are present in the members of the tribe Viciae examined. Sequence analysis and 3D modelling indicates that p54 proteins belong to the cupin superfamily, and that they are related to sucrose binding proteins and, to a lesser extent, to vicilin-type seed storage proteins. Nevertheless, several distinctive characteristics of psp54 expression have been found: (i) the gene is differentially induced by ABA and several stress situations, in accordance with the presence of putative separate ABA and stress responsive elements in its promoter; (ii) the proteins are present in pods and seed coats, tissues of maternal origin; and (iii) p54 mRNA accumulates in the dry seeds. In view of both the functional properties of p54-derived proteins and the features of the psp54 gene expression, it is concluded that p54 represents a novel class within the cupin superfamily.

Keywords: Abscisic acid; ABA; cupins; pea seed germination; processing of precursor peptides; protein modelling; stress-induced gene expression.
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A. P. Gagete, M. Riera, L. Franco, and M. I. Rodrigo
Functional analysis of the isoforms of an ABI3-like factor of Pisum sativum generated by alternative splicing
J. Exp. Bot., April 1, 2009; 60(6): 1703 - 1714.
[Abstract] [Full Text] [PDF]


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