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Multiple forms of α-glucosidase in rice seeds (Oryza sativa L., var Nipponbare)

机译:水稻种子中的多种形式的α-葡萄糖苷酶(Oryza sativa L.,var Nipponbare)

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摘要

Two isoforms of α-glucosidases (ONG2-I and ONG2-II) were purified from dry rice seeds (Oryza sativa L., var Nipponbare). Both ONG2-I and ONG2-II were the gene products of ONG2 mRNA expressed in ripening seeds. Each enzyme consisted of two components of 6 kDa-peptide and 88 kDa-peptide encoded by this order in ONG2 cDNA (ong2), and generated by post-translational proteolysis. The 88 kDa-peptide of ONG2-II had 10 additional N-terminal amino acids compared with the 88 kDa-peptide of ONG2-I. The peptides between 6 kDa and 88 kDa components (26 amino acids for ONG2-I and 16 for ONG2-II) were removed by post-translational proteolysis. Proteolysis induced changes in adsorption and degradation of insoluble starch granules. We also obtained three α-glucosidase cDNAs (ong1, ong3, and ong4) from ripening seeds. The ONG1, ONG2, and ONG4 genes were situated in distinct locus of rice genome. The transcripts encoding ONG2 and ONG3 were generated by alternative splicing. Members of α-glucosidase multigene family are differentially expressed during ripening and germinating stages in rice.
机译:从干稻种子(Oryza sativa L.,var Nipponbare)中纯化了两种α-葡萄糖苷酶同工型(ONG2-I和ONG2-II)。 ONG2-I和ONG2-II都是在成熟种子中表达的ONG2 mRNA的基因产物。每种酶均由ONG2 cDNA(ong2)中的该顺序编码的6 kDa肽和88 kDa肽的两个成分组成,并通过翻译后蛋白水解产生。与ONG2-I的88 kDa肽相比,ONG2-II的88 kDa肽具有10个额外的N末端氨基酸。通过翻译后蛋白水解除去6 kDa和88 kDa组分之间的肽(ONG2-I为26个氨基酸,ONG2-II为16个氨基酸)。蛋白水解引起不溶性淀粉颗粒的吸附和降解变化。我们还从成熟的种子中获得了三个α-葡萄糖苷酶cDNA(ong1,ong3和ong4)。 ONG1,ONG2和ONG4基因位于水稻基因组的不同位点。编码ONG2和ONG3的转录本是通过选择性剪接产生的。在水稻的成熟和发芽阶段,α-葡萄糖苷酶多基因家族的成员差异表达。

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