75 research outputs found
รายงานการวิจัยการบ่งชี้และศึกษาการทำงานของจิบเบอริลินเบตากูลโคไซเดสจากข้าว
Funded by Suranaree University of Technology budget year 2012-201
Genomic and expression analysis of glycosyl hydrolase family 35 genes from rice (Oryza sativa L.)
<p>Abstract</p> <p>Background</p> <p>Many plant β-galactosidases (Bgals) have been well characterized and their deduced biological functions mainly involve degradation of structural pectins, xyloglucans or arabinogalactoproteins in plant cell walls. However, gene multiplicity in glycosyl hydrolase family 35 (GH35), to which these proteins belong, implies diverse functions. In this study, the gene multiplicity, apparent evolutionary relationships and transcript expression of rice Bgal genes were examined, in order to predict their biological functions.</p> <p>Results</p> <p>Fifteen rice Bgal genes were identified in the plant genome, one of which encodes a protein similar to animal Bgals (<it>OsBgal9</it>), and the remaining 14 fall in a nearly plant-specific subfamily of Bgals. The presence of both classes of Bgals in bryophytes, as well as vascular plants, suggests both gene lineages were present early in plant evolution. All 15 proteins were predicted to contain secretory signal sequences, suggesting they have secretory pathway or external roles. RT-PCR and database analysis found two distinct lineages to be expressed nearly exclusively in reproductive tissues and to be closely related to <it>Arabidopsis </it>Bgals expressed most highly in flower and pollen. On the other hand, <it>OsBgal6 </it>is expressed primarily in young vegetative tissues, and alternative splicing in panicle prevents its production of full-length protein in this reproductive tissue. <it>OsBgal11 </it>also showed alternative splicing to produce different length proteins. OsBgal13 produced by recombinant expression in <it>Escherichia coli </it>hydrolyzed α-L-arabinoside in addition to β-D-galactoside and β-(1→3)-, β-(1→4)- and β-(1→6)- linked galacto-oligosaccharides.</p> <p>Conclusion</p> <p>Rice <it>GH35 </it>contains fifteen genes with a diversity of protein sequences, predicted locations and expression and splicing patterns that suggest that OsBgals enzymes may play a variety of roles in metabolism of cell wall polysaccharides, glycoproteins and glycolipids.</p
Editorial: Advances in metabolism and chemodiversity – focus – anthocyanin and proanthocyanin: biosynthesis, accumulation, regulation
Analysis of rice glycosyl hydrolase family 1 and expression of Os4bglu12 β-glucosidase
BACKGROUND: Glycosyl hydrolase family 1 (GH1) β-glucosidases have been implicated in physiologically important processes in plants, such as response to biotic and abiotic stresses, defense against herbivores, activation of phytohormones, lignification, and cell wall remodeling. Plant GH1 β-glucosidases are encoded by a multigene family, so we predicted the structures of the genes and the properties of their protein products, and characterized their phylogenetic relationship to other plant GH1 members, their expression and the activity of one of them, to begin to decipher their roles in rice. RESULTS: Forty GH1 genes could be identified in rice databases, including 2 possible endophyte genes, 2 likely pseudogenes, 2 gene fragments, and 34 apparently competent rice glycosidase genes. Phylogenetic analysis revealed that GH1 members with closely related sequences have similar gene structures and are often clustered together on the same chromosome. Most of the genes appear to have been derived from duplications that occurred after the divergence of rice and Arabidopsis thaliana lineages from their common ancestor, and the two plants share only 8 common gene lineages. At least 31 GH1 genes are expressed in a range of organs and stages of rice, based on the cDNA and EST sequences in public databases. The cDNA of the Os4bglu12 gene, which encodes a protein identical at 40 of 44 amino acid residues with the N-terminal sequence of a cell wall-bound enzyme previously purified from germinating rice, was isolated by RT-PCR from rice seedlings. A thioredoxin-Os4bglu12 fusion protein expressed in Escherichia coli efficiently hydrolyzed β-(1,4)-linked oligosaccharides of 3–6 glucose residues and laminaribiose. CONCLUSION: Careful analysis of the database sequences produced more reliable rice GH1 gene structure and protein product predictions. Since most of these genes diverged after the divergence of the ancestors of rice and Arabidopsis thaliana, only a few of their functions could be implied from those of GH1 enzymes from Arabidopsis and other dicots. This implies that analysis of GH1 enzymes in monocots is necessary to understand their function in the major grain crops. To begin this analysis, Os4bglu12 β-glucosidase was characterized and found to have high exoglucanase activity, consistent with a role in cell wall metabolism
Bacterial β-Glucosidase Reveals the Structural and Functional Basis of Genetic Defects in Human Glucocerebrosidase 2 (GBA2)
Human glucosylcerebrosidase 2 (GBA2) of the CAZy family GH116 is responsible for the breakdown of glycosphingolipids on the cytoplasmic face of the endoplasmic reticulum and Golgi apparatus. Genetic defects in GBA2 result in spastic paraplegia and cerebellar ataxia, while cross-talk between GBA2 and GBA1 glucosylceramidases may affect Gaucher disease. Here, we report the first three-dimensional structure for any GH116 enzyme, Thermoanaerobacterium xylanolyticum TxGH116 β-glucosidase, alone and in complex with diverse ligands. These structures allow identification of the glucoside binding and active site residues, which are shown to be conserved with GBA2. Mutagenic analysis of TxGH116 and structural modeling of GBA2 provide a detailed structural and functional rationale for pathogenic missense mutations of GBA2
รายงานการวิจัยการวิเคราะห์หน้าที่ของเอนไซม์โมโนลิกนอล เบต้า-กลูโคซิเดส จากข้าว
Funded by Suranaree University of Technology budget year 201
รายงานการวิจัย การศึกษาการทำงานของไกลโคไซด์ไฮโดรเลส ตระกูลที่1 กลุ่ม6
Funded by Suranaree University of Technology budget year 201
รายงานการวิจัยการตรวจหาด้วยเอนไซม์และการศึกษาสารประเภทไกลโคไซด์จากพืชไทย
Suranaree University of Technolog
รายงานการวิจัยการแสดงลักษณะเฉพาะของไกลโคซิเดสจากพืชตระกูลถั่วป่า
ผลงานวิชาการคณาจารย์มหาวิทยาลัยเทคโนโลยีสุรนาร
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