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Diversity of the superfamily ofphloem lectins (phloem protein 2) in angiosperms

Author:
Dinant, S., Clark, A.M., Zhu, Y., Vilaine, F., Palauqui, J.C., Kusiak, C., Thompson, G.A.
Source:
Plant physiology 2003 v.131 no.1 pp. 114-128
ISSN:
0032-0889
Subject:
RNA-binding proteins, phylogeny, plant proteins, celery, hypocotyls, gene expression, leaves, Apium graveolens, Arabidopsis thaliana, messenger RNA, Cucumis sativus, Cucumis melo, cucumbers, conserved sequences, amino acid sequences, Cucumis metuliferus, phloem, chitin, lectins, gene duplication, nucleotide sequences, chemical constituents of plants, plant morphology
Abstract:
Phloem protein 2 (PP2) is one of the most abundant and enigmatic proteins in the phloem sap. Although thought to be associated with structural P-protein, PP2 is translocated in the assimilate stream where its lectin activity or RNA-binding properties can exert effects over long distances. Analyzing the diversity of these proteins in vascular plants led to the identification of PP2-like genes in species from 17 angiosperm and gymnosperm genera. This wide distribution of PP2 genes in the plant kingdom indicates that they are ancient and common in vascular plants. Their presence in cereals and gymnosperms, both of which lack structural P-protein, also supports a wider role for these proteins. Within this superfamily, PP2 proteins have considerable size polymorphism. This is attributable to variability in the length of the amino terminus that extends from a highly conserved domain. The conserved PP2 domain was identified in the proteins encoded by six genes from several cucurbits, celery (Apium graveolens), and Arabidopsis that are specifically expressed in the sieve element-companion cell complex. The acquisition of additional modular domains in the amino-terminal extensions of other PP2-like proteins could reflect divergence from its phloem function.
Agid:
671589