Abstract
Glycine-rich proteins (GRPs) are a group of proteins characterized by their high content of glycine residues often occurring in repetitive blocs. The diverse expression pattern and sub cellular localization of various GRPs suggest their implication in different physiological processes. Several GRPs has been isolated and characterized from different monocots and dicots. However, little or no information is available about the structure and function of GRPs in asexually reproducing plants. In this study, in-silico analysis of expressed sequence tag database resulted in the isolation of fifty-one GRPs from Curcuma longa L., an asexually reproducible plant of great medicinal and economic significance. Phylogenetic analysis grouped the GRPs into four distinct classes based on conserved motifs and nature of glycine-rich repeats. Majority of the isolated GRPs exhibited high homology with known GRPs from other plants that are expressed in response to various stresses. The presence of high structural diversity and signal peptide in some GRPs suggest their diverse physiological role and tissue specific localization. The isolated sequences can be used as a framework for cloning, characterization and expressional analysis of GRPs in response to various biotic and abiotic stresses in Curcuma longa as well as other asexually reproducing plants.
Highlights
The glycine rich proteins (GRPs) belong to a group of super family that is characterized by the presence of semi-repetitive glycine-rich motifs
Eleven of the 14 class I GRPs showed the presence of a signal peptide at their N-terminal end suggesting their location in the cell wall or cell membrane
Similar results were retrieved in Eucalyptus GRPs [16].Searching the turmeric expressed sequence tags (ESTs) database using the previously reported GRPs with cysteine rich domans and C terminal homology to nodulins resulted in the identification of five GRPs with GGXXXGG repeats
Summary
The glycine rich proteins (GRPs) belong to a group of super family that is characterized by the presence of semi-repetitive glycine-rich motifs. These groups of proteins have a glycine content of 20 to 70% that are arranged in (Gly)n-X repetitions. The class I GRPs contain a signal peptide followed by a high glycine-content region with (GGX)n repeats. These proteins are attributed with structural function due to their cell wall localization [2]. Class III GRPs may carry a signal peptide and have the lowest glycine content as compared to other classes They are charactrized by the presence of GXGX repeats and show a high degree of structural diversity. A few of the RNA binding GRPs are characterized by the presence of CCHC zinc-fingers in their structure
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