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首页> 外文期刊>Current Genetics >cDNA encoding protein O-mannosyltransferase from the filamentous fungus Trichoderma reesei; functional equivalence to Saccharomyces cerevisiae PMT2
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cDNA encoding protein O-mannosyltransferase from the filamentous fungus Trichoderma reesei; functional equivalence to Saccharomyces cerevisiae PMT2

机译:编码丝状真菌里氏木霉的蛋白O-甘露糖基转移酶的cDNA;与酿酒酵母PMT2的功能等效

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摘要

O-Mannosylation is suggested to be essential for protein secretion in Trichoderma reesei. In protein O-glycosylation, the first mannosyl residue is transferred to a serine or threonine hydroxyl group of the protein from dolichyl phosphate mannose by protein O-mannosyltransferase. In Saccharomyces cerevisiae, seven PMT genes have been cloned coding for these enzymes. In the present work, the characterisation of the pmt1 cDNA from T. reesei is reported. Sequence analysis of the predicted protein revealed the highest similarity to Schizosaccharomyces pombe Pmt and to Pmt4p of Saccharomyces cerevisiae. In contrast, expression of the T. reesei cDNA in various S. cerevisiae pmt mutants showed functional similarity to the yeast Pmt2 protein.
机译:建议O-甘露糖基化对于里氏木霉中的蛋白质分泌是必不可少的。在蛋白质O-糖基化中,通过蛋白质O-甘露糖基转移酶将第一个甘露糖基残基从二聚磷酸磷酸甘露糖转移至蛋白质的丝氨酸或苏氨酸羟基。在酿酒酵母中,已经克隆了七个编码这些酶的PMT基因。在目前的工作中,报道了来自里氏木霉的pmt1 cDNA的表征。预测蛋白质的序列分析显示与粟酒裂殖酵母Pmt和酿酒酵母Pmt4p的最高相似性。相反,里氏木霉cDNA在多种酿酒酵母pmt突变体中的表达显示出与酵母Pmt2蛋白的功能相似性。

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