title: Putative fasciclin-like arabinogalactan-proteins (FLA) in wheat (Triticum aestivum) and rice (Oryza sativa): identification and bioinformatic analyses.
abstract: Putative plant adhesion molecules include arabinogalactan-proteins having fasciclin-like domains. In animal, fasciclin proteins participate in cell adhesion and communication. However, the molecular basis of interactions in plants is still unknown and none of these domains have been characterized in cereals. This work reports the characterization of 34 wheat (Triticum aestivum) and 24 rice (Oryza sativa) Fasciclin-Like Arabinogalactan-proteins (FLAs). Bioinformatics analyses show that cereal FLAs share structural characteristics with known Arabidopsis FLAs including arabinogalactan-protein and fasciclin conserved domains. At least 70% of the wheat and rice FLAs are predicted to be glycosylphosphatidylinositol-anchored to the plasma membranes. Expression analyses determined from the relative abundance of ESTs in the publicly available wheat EST databases and from RNA gel blots indicate that most of these genes are weakly expressed and found mainly in seeds and roots. Furthermore, most wheat genes were down regulated by abiotic stresses except for TaFLA9 and 12 where cold treatment induces their expression in roots. Plant fasciclin-like domains were predicted to have 3-D homology with FAS1 domain of the fasciclin I insect neural cell adhesion molecule with an estimated precision above 70%. The structural analysis shows that negatively charged amino acids are concentrated along the beta1-alpha3-alpha4-beta2 edges, while the positively charged amino acids are concentrated on the back side of the folds. This highly charged surface distribution could provide a way of mediating protein-protein interactions via electrostatic forces similar to many other adhesion molecules. The identification of wheat FLAs will facilitate studying their function in plant growth and development and their role in stress response.
authors.affiliation: Department of Environmental and Plant Biology, Ohio University, Porter Hall, Athens, OH 45701, USA. faik@ohio.edu
authors.forename: Ahmed
authors.initials: A
authors.lastname: Faik
authors.forename: Jaouad
authors.initials: J
authors.lastname: Abouzouhair
authors.forename: Fathey
authors.initials: F
authors.lastname: Sarhan
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D019295:Computational Biology; D017931:DNA Primers; D008969:Molecular Sequence Data; D009088:Mucoproteins / Q000235:genetics*; D012275:Oryza / Q000235:genetics*; D010940:Plant Proteins / Q000235:genetics; D016133:Polymerase Chain Reaction; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D014908:Triticum / Q000235:genetics*
chemical_list: D017931:DNA Primers; D009088:Mucoproteins; D010940:Plant Proteins; C006619:arabinogalactan proteins