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酿酒酵母外链甘露聚糖中形成和延伸甘露糖分支所需的MNN2和MNN5甘露糖基转移酶的鉴定。

Identification of the MNN2 and MNN5 mannosyltransferases required for forming and extending the mannose branches of the outer chain mannans of Saccharomyces cerevisiae.

作者信息

Rayner J C, Munro S

机构信息

Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, United Kingdom.

出版信息

J Biol Chem. 1998 Oct 9;273(41):26836-43. doi: 10.1074/jbc.273.41.26836.

Abstract

The mannan structure found on the N-linked glycans of the yeast Saccharomyces cerevisiae is composed of a long backbone of alpha-1, 6-linked mannose to which are attached branches consisting of two alpha-1,2-linked mannoses followed by an alpha-1,3-linked mannose. In the mutants mnn2 and mnn5, the addition of the first and second of these two mannoses, respectively, is defective. In this paper, we report the identification of the genes corresponding to these mutations. The two genes encode closely related proteins with distant homology to the known Mnn1p alpha-1,3-mannosyltransferase. We show that these proteins are localized in an early compartment of the yeast Golgi and that they are not physically associated with each other or with the two protein complexes known to be involved in synthesizing the alpha-1,6-linked backbone. The identification of Mnn2p and Mnn5p allows us to assign Golgi proteins to all of the catalytic steps in S. cerevisiae mannan synthesis.

摘要

在酿酒酵母N-连接聚糖上发现的甘露聚糖结构由一条长的α-1,6-连接的甘露糖主链组成,主链上连接着由两个α-1,2-连接的甘露糖和一个α-1,3-连接的甘露糖组成的分支。在突变体mnn2和mnn5中,这两个甘露糖中第一个和第二个的添加分别存在缺陷。在本文中,我们报告了与这些突变相对应的基因的鉴定。这两个基因编码的蛋白质与已知的Mnn1pα-1,3-甘露糖基转移酶具有远缘同源性且密切相关。我们表明,这些蛋白质定位于酵母高尔基体的早期区室,并且它们彼此之间或与已知参与合成α-1,6-连接主链的两种蛋白质复合物没有物理关联。Mnn2p和Mnn5p的鉴定使我们能够将高尔基体蛋白分配到酿酒酵母甘露聚糖合成的所有催化步骤中。

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