Structural characterization of the Get4/Get5 complex and its interaction with Get3
Structural characterization of the Get4/Get5 complex and its interaction with Get3
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DOI：
10.1073/pnas.1006036107
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发表时间：
2010-07-06
影响因子：
11.1
通讯作者：
Clemons, William M., Jr.
中科院分区：
文献类型：
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作者：
Chartron, Justin W.;Suloway, Christian J. M.;Clemons, William M., Jr.
最近阐明的Get蛋白负责将大多数尾锚定（TA）蛋白靶向递送至内质网。已经在介导TA底物递送至细胞质靶向因子Get 3的途径的早期步骤中鉴定了Get 4和Get 5。在这里，我们报告的晶体结构的Get 4和Get 5的N-末端片段从酿酒酵母。我们发现Get 4和Get 5（Get 4/5）形成了一个紧密的复合物，它以二聚体（Get 4/5的两个拷贝）的形式存在，由Get 5的C-末端介导。我们进一步证明，Get 3特异性地结合到Get 4上的保守表面上的核苷酸依赖性方式。这项工作提供了一个模型，其中Get 4/5操作Get 3的上游和介导的TA基板的具体交付的进一步证据。
The recently elucidated Get proteins are responsible for the targeted delivery of the majority of tail-anchored (TA) proteins to the endoplasmic reticulum. Get4 and Get5 have been identified in the early steps of the pathway mediating TA substrate delivery to the cytoplasmic targeting factor Get3. Here we report a crystal structure of Get4 and an N-terminal fragment of Get5 from Saccharomyces cerevisae. We show Get4 and Get5 (Get4/5) form an intimate complex that exists as a dimer (two copies of Get4/5) mediated by the C-terminus of Get5. We further demonstrate that Get3 specifically binds to a conserved surface on Get4 in a nucleotide dependent manner. This work provides further evidence for a model in which Get4/5 operates upstream of Get3 and mediates the specific delivery of a TA substrate.