Crystal Structure of Get4-Get5 Complex and Its Interactions with Sgt2, Get3, and Ydj1
Crystal Structure of Get4-Get5 Complex and Its Interactions with Sgt2, Get3, and Ydj1
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DOI：
10.1074/jbc.m109.087098
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发表时间：
2010-03-26
影响因子：
4.8
通讯作者：
Wang, Chung
中科院分区：
文献类型：
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作者：
Chang, Yi-Wei;Chuang, Yi-Chien;Wang, Chung
酿酒酵母中的Get 3、Get 4和Get 5参与将尾锚定蛋白插入内质网膜。我们阐明了Get 4和Get 5之间的相互作用，并研究了它们与Get 3和一种含有三肽重复序列的蛋白质Sgt 2的相互作用。基于免疫共沉淀和晶体学研究，Get 4和Get 5形成紧密复合物，表明它们构成更大复合物的亚基。相反，虽然Get 3与Get 4-Get 5复合物物理相互作用，但少量的Get 3与Get 5共沉淀，这意味着Get 3和Get 4-Get 5之间的瞬时相互作用。Sgt 2也与Get 5相互作用，尽管与Get 5共沉淀的Sgt 2的量变化。此外，GET 3，GET 4和GET 5与分子伴侣YDJ 1发生遗传相互作用，表明分子伴侣也可能参与尾锚定蛋白的插入。
Get3, Get4, and Get5 in Saccharomyces cerevisiae participate in the insertion of tail-anchored proteins into the endoplasmic reticulum membrane. We elucidated the interaction between Get4 and Get5 and investigated their interaction with Get3 and a tetratricopeptide repeat-containing protein, Sgt2. Based on co-immunoprecipitation and crystallographic studies, Get4 and Get5 formed a tight complex, suggesting that they constitute subunits of a larger complex. In contrast, although Get3 interacted physically with the Get4-Get5 complex, low amounts of Get3 co-precipitated with Get5, implying a transient interaction between Get3 and Get4-Get5. Sgt2 also interacted with Get5, although the amount of Sgt2 that co-precipitated with Get5 varied. Moreover, GET3, GET4, and GET5 interacted genetically with molecular chaperone YDJ1, suggesting that chaperones might also be involved in the insertion of tail-anchored proteins.