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本文引用的文献

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Processing of X-ray diffraction data collected in oscillation mode.振荡模式下收集的X射线衍射数据的处理。
Methods Enzymol. 1997;276:307-26. doi: 10.1016/S0076-6879(97)76066-X.
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Biogenesis of tail-anchored proteins: the beginning for the end?尾部锚定蛋白的生物发生:结束的开始?
J Cell Sci. 2009 Oct 15;122(Pt 20):3605-12. doi: 10.1242/jcs.041210.
3
Comprehensive characterization of genes required for protein folding in the endoplasmic reticulum.内质网中蛋白质折叠所需基因的全面表征。
Science. 2009 Mar 27;323(5922):1693-7. doi: 10.1126/science.1167983.
4
Prm3p is a pheromone-induced peripheral nuclear envelope protein required for yeast nuclear fusion.Prm3p是酵母细胞核融合所需的一种信息素诱导的外周核膜蛋白。
Mol Biol Cell. 2009 May;20(9):2438-50. doi: 10.1091/mbc.e08-10-0987. Epub 2009 Mar 18.
5
Structural and functional characterization of human SGT and its interaction with Vpu of the human immunodeficiency virus type 1.人SGT的结构与功能特性及其与人免疫缺陷病毒1型Vpu的相互作用
Biochemistry. 2008 Sep 23;47(38):10123-31. doi: 10.1021/bi800758a. Epub 2008 Aug 30.
6
The GET complex mediates insertion of tail-anchored proteins into the ER membrane.GET复合体介导尾锚定蛋白插入内质网(ER)膜。
Cell. 2008 Aug 22;134(4):634-45. doi: 10.1016/j.cell.2008.06.025.
7
High-quality binary protein interaction map of the yeast interactome network.酵母相互作用组网络的高质量二元蛋白质相互作用图谱。
Science. 2008 Oct 3;322(5898):104-10. doi: 10.1126/science.1158684. Epub 2008 Aug 21.
8
A precursor-specific role for Hsp40/Hsc70 during tail-anchored protein integration at the endoplasmic reticulum.热休克蛋白40/热休克蛋白70在尾锚定蛋白在内质网整合过程中的前体特异性作用。
J Biol Chem. 2008 Oct 10;283(41):27504-27513. doi: 10.1074/jbc.M804591200. Epub 2008 Jul 29.
9
The chemical genomic portrait of yeast: uncovering a phenotype for all genes.酵母的化学基因组图谱:揭示所有基因的表型
Science. 2008 Apr 18;320(5874):362-5. doi: 10.1126/science.1150021.
10
Genomic, evolutionary, and expression analyses of cee, an ancient gene involved in normal growth and development.cee的基因组、进化及表达分析,cee是一个参与正常生长和发育的古老基因。
Genomics. 2008 Apr;91(4):315-25. doi: 10.1016/j.ygeno.2007.10.017. Epub 2008 Jan 31.

Get4-Get5 复合物的晶体结构及其与 Sgt2、Get3 和 Ydj1 的相互作用。

Crystal structure of Get4-Get5 complex and its interactions with Sgt2, Get3, and Ydj1.

机构信息

Institute of Molecular Biology, Academia Sinica, Taipei 115; Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu 300.

Institute of Molecular Biology, Academia Sinica, Taipei 115.

出版信息

J Biol Chem. 2010 Mar 26;285(13):9962-9970. doi: 10.1074/jbc.M109.087098. Epub 2010 Jan 27.

DOI:10.1074/jbc.M109.087098
PMID:20106980
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2843242/
Abstract

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.

摘要

在酿酒酵母中,Get3、Get4 和 Get5 参与将尾部锚定蛋白插入内质网膜的过程。我们阐明了 Get4 和 Get5 之间的相互作用,并研究了它们与 Get3 和含有四肽重复的 Sgt2 蛋白之间的相互作用。基于免疫共沉淀和晶体学研究,Get4 和 Get5 形成了紧密的复合物,表明它们构成了更大复合物的亚基。相比之下,尽管 Get3 与 Get4-Get5 复合物在物理上相互作用,但只有少量的 Get3 与 Get5 共沉淀,这表明 Get3 和 Get4-Get5 之间存在瞬时相互作用。Sgt2 也与 Get5 相互作用,尽管与 Get5 共沉淀的 Sgt2 量有所不同。此外,GET3、GET4 和 GET5 在遗传上与分子伴侣 YDJ1 相互作用,表明伴侣蛋白也可能参与尾部锚定蛋白的插入过程。