ABSTRACT
Isozymes of glycosyl hydrolase Family 17 hydrolyze 1,3-beta-glucan polysaccharides found in the cell wall matrix of plants and fungi, enabling these plant enzymes to serve diverse roles in plant defense and plant development. Fourteen genes from Family 17 have been characterized in the genome of rice. A sequence dendrogram analysis divided these genes into four subfamilies. The recombinant GNS1 enzyme from subfamily B had 1,3;1,4-beta-glucanase activity, suggesting a role for this isozyme in plant development.
Subject(s)
Glucans/metabolism , Glycoside Hydrolases/genetics , Glycoside Hydrolases/metabolism , Oryza/genetics , Amino Acid Sequence , Evolution, Molecular , Genes, Plant , Glucans/chemistry , Glycoside Hydrolases/chemistry , Isoenzymes/chemistry , Isoenzymes/genetics , Isoenzymes/metabolism , Molecular Sequence Data , Oryza/enzymology , Phylogeny , Plants/enzymology , Recombinant Proteins/metabolism , Sequence Alignment , Sequence Homology, Amino AcidABSTRACT
Thirteen new beta-glucanase-encoding genes have been identified in the rice genome. These genes, together with other monocot beta-glucanases, have now been classified into four subfamilies based on the structure and function of the genes. Two tandem gene clusters, Gns2-Gns3-Gns4 and Gns5-Gns6, were classified in the defense-related Subfamily A. Growth-related 1,3;1,4-beta-glucanase Gns1 was classified in Subfamily B. Gns7 and Gns8, together with the barley genes GVI and Hv34, represent Subfamily C. Gns9 and a beta-glucanase gene from wheat were grouped in Subfamily D. Genes in Subfamilies C and D have structures that are distinct from those of the other subfamilies, but there are very little data available on the biochemical or physiological roles of these genes. Gene expression in growing tissues and lack of gene induction in response to disease-related treatments suggest that Subfamilies C and D may function in control of plant growth.
Subject(s)
Glycoside Hydrolases/genetics , Multigene Family , Oryza/enzymology , Oryza/genetics , Amino Acid Sequence , Gene Expression Regulation, Plant , Glucan Endo-1,3-beta-D-Glucosidase/genetics , Molecular Sequence Data , Plant Proteins/genetics , Sequence Analysis, DNA , Transcriptional ActivationABSTRACT
Enzyme electrophoresis was used to compare the isozyme phenotypes of Oryza sativa, IR31917 (AA genome), and two O. minuta accessions (Om 101089 and Om101141; BBCC genome) for ten enzyme systems. Between the two species, two systems were monomorphic (isocitrate dehydrogenase and alcohol dehydrogenase) and eight were polymorphic (shikimate dehydrogenase, phosphogluconate dehydrogenase, phosphoglucose isomerase, malate dehydrogenase, glutamate oxaloacetate transaminase, esterase, aminopeptidase, and endopeptidase). Polymorphism between O. minuta accessions was detected for shikimate dehydrogenase and glutamate oxaloacetate. As expected, the quaternary structure of the O. minuta isozymes was comparable to that of O. sativa. Possible allelic relationships with known O. sativa alleles and their genomic designation are discussed. Combined with chromosome data, the interspecific variation was exploited to monitor the relative genetic contribution of the two parents in the IR31917/Om101141 F1 hybrids and recurrent (IR31917) backcross progenies. The isozyme content of F1 hybrid reflected its triploid nature (ABC genome composition), while that of the backcross progenies paralleled the duplication of the A genome and the gradual loss of O. minuta chromosomes during the backcrossing process. Evidence is provided for a degree of homoeology between the A, B, and C genomes, and for introgression from O. minuta into O. sativa.
