Oligosaccharyltransferase: a complex multisubunit enzyme of the endoplasmic reticulum.
Oligosaccharyltransferase: a complex multisubunit enzyme of the endoplasmic reticulum.
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寡糖转移酶：内质网的一种复杂的多亚基酶。
DOI：
10.1006/bbrc.1999.1886
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发表时间：
1999
期刊：
影响因子：
--
通讯作者：
Lennarz,WJ
中科院分区：
文献类型：
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作者：
Yan,Q;Lennarz,WJ
N-连接寡糖链与蛋白质的连接是一个重要的共翻译过程。在某些情况下，这些链可以用于稳定蛋白质，而在其他情况下，它们作为识别元件发挥作用。N-糖基化过程中的关键酶是寡糖基转移酶（OT）。在酵母中，这种存在于内质网中的酶由九种不同的跨膜蛋白亚基组成。我们的总体目标是更多地了解酵母OT的多个亚基的功能及其相互作用的模式。使用生物化学和遗传技术的组合，亚基Ost 1 p已被证明识别Asn-X-Ser/Thr糖基化位点。鉴定过程中使用的主要工具是基于二苯甲酮的糖基化位点肽，其显示与Ost 1 p交联。我们目前的目标是确定参与识别糖基化位点序列的一级结构中的结构域。通过使用双功能交联剂，Ost 1 p与OT的其他亚基的可能的相互作用将被研究。本文对OT亚基的研究工作和其他研究进行了简要的总结。
The attachment of N-linked oligosaccharide chains to proteins is an important cotranslational process. These chains can, in some cases, serve to stabilize the protein, while in other cases they function as recognition elements. A key enzyme in the N-glycosylation process is oligosaccharyltransferase (OT). In yeast this enzyme, which is found in the endoplasmic reticulum, consists of nine different transmembrane protein subunits. Our general aim is to learn more about the functions of the multiple subunits of yeast OT and their mode of interaction with each other. Using a combination of biochemical and genetic techniques the subunit Ost1p has been shown to recognize Asn-X-Ser/Thr glycosylation sites. The principle tool used in the identification process was a benzophenone-based glycosylation site peptide that was shown to be crosslinked to Ost1p. Our current objective is to identify the domain in the primary structure that is involved in recognition of the glycosylation site sequence. By use of bifunctional crosslinkers, the possible interaction of Ost1p with other subunits of OT will be studied. This work and other studies on the OT subunits are concisely summarized.