Abstract
The occurrence of quasi-repetitive glycine-rich peptides has been reported in different organisms. Glycine-rich regions are proposed to be involved in protein-protein interactions in some mammalian protein families. In plants, a set of glycine-rich proteins (GRPs) was characterized several years ago, and since then a wealth of new GRPs have been identified. GRPs may have very diverse sub-cellular localization and functions. The only common feature among all different GRPs is the presence of glycine-rich repeat domains. The expression of genes encoding GRPs is developmentally regulated, and also induced, in several plant genera, by physical, chemical and biological factors. In addition to the highly modulated expression, several GRPs also show tissue-specific localization. GRPs specifically expressed in xylem, phloem, epidermis, anther tapetum and roots have been described. In this paper, the structural and functional features of these proteins in Eucalyptus are summarized. Since this is the first description of GRPs in this species, particular emphasis has been given to the expression pattern of these genes by analyzing their abundance and prevalence in the different cDNA-libraries of the Eucalyptus Genome Sequencing Project Consortium (ForEST). The comparison of GRPs from Eucalyptus and other species is also discussed.
Highlights
Glycine-rich proteins (GRPs) are characterized by the presence of domains that show little sequence conservation and are highly enriched in residues of the amino acid glycine
The diverse but highly specific expression pattern of grp genes, taken together with the distinct sub-cellular localization of some glycine-rich proteins (GRPs) groups, clearly indicate that these proteins are implicated in several independent physiological processes (Condit, 1993; Keller and Heierli, 1994; Sachetto-Martins et al, 1995; Magioli et al, 2001; Franco et al, 2002)
The complete list of sequences used as baits include the 86 proteins reviewed in Sachetto-Martins et al (2000), 8 sequences recently described from a complete survey of Arabidopsis glycine-rich RNA binding proteins (Lorkovic and Barta, 2002), a wheat cold shock domain GRP (Karlson et al, 2002), a Pinus taeda cell wall GRP (Allona et al, 1998), Figure 1 - Schematic representation of the domain organization of plant glycine-rich proteins (GRPs)
Summary
Glycine-rich proteins (GRPs) are characterized by the presence of domains that show little sequence conservation and are highly enriched in residues of the amino acid glycine. These Glycine-rich domains are arranged in (Gly)n-X repetitions. The first genes encoding GRPs have been isolated from plants, proteins with characteristic repetitive glycine stretches have been reported in a wide variety of organisms from cyanobacterias to animals (reviewed in Sachetto-Martins et al, 2000). These characteristics were the most intensively studied aspects of GRP genes since they point to the possible biotechnological application of their promoters
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