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首页> 外文期刊>Cellular & molecular biology letters. >Non-erythroid beta spectrin interacting proteins and their effects on spectrin tetramerization.
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Non-erythroid beta spectrin interacting proteins and their effects on spectrin tetramerization.

机译：非类胡萝卜素β血影蛋白相互作用蛋白及其对血影蛋白四聚化的影响。

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摘要

With yeast two-hybrid methods, we used a C-terminal fragment (residues 1697-2145) of non-erythroid beta spectrin (betaII-C), including the region involved in the association with alpha spectrin to form tetramers, as the bait to screen a human brain cDNA library to identify proteins interacting with betaII-C. We applied stringent selection steps to eliminate false positives and identified 17 proteins that interacted with betaII-C (IP(betaII-C) s). The proteins include a fragment (residues 38-284) of "THAP domain containing, apoptosis associated protein 3, isoform CRA g", "glioma tumor suppressor candidate region gene 2" (residues 1-478), a fragment (residues 74-442) of septin 8 isoform c, a fragment (residues 704-953) of "coatomer protein complex, subunit beta 1, a fragment (residues 146-614) of zinc-finger protein 251, and a fragment (residues 284-435) of syntaxin binding protein 1. We used yeast three-hybrid system to determine the effects of these betaII-C interacting proteins as well as of 7 proteins previously identified to interact with the tetramerization region of non-erythroid alpha spectrin (IP(alphaII-N) s) [1] on spectrin tetramer formation. The results showed that 3 IP(betaII-C) s were able to bind betaII-C even in the presence of alphaII-N, and 4 IP(alphaII-N) s were able to bind alphaII-N in the presence of betaII-C. We also found that the syntaxin binding protein 1 fragment abolished alphaII-N and betaII-C interaction, suggesting that this protein may inhibit or regulate non-erythroid spectrin tetramer formation.
机译：通过酵母双杂交方法，我们使用了非类胡萝卜素β血影蛋白（betaII-C）的C末端片段（1697-2145位残基），包括与α血影蛋白结合形成四聚体的区域，作为诱饵。筛选人脑cDNA文库以鉴定与betaII-C相互作用的蛋白质。我们应用了严格的选择步骤来消除假阳性，并鉴定了与betaII-C（IP（betaII-C）s）相互作用的17种蛋白质。所述蛋白质包括“含有THAP结构域，凋亡相关蛋白3，同工型CRA g”，“神经胶质瘤肿瘤抑制候选区域基因2”的片段（残基38-284）（残基1-478），片段（残基74-442）。 ），Septin 8同工型c，“涂层蛋白复合物的片段（704-953残基），β1亚基，锌指蛋白251的片段（146-614残基）和锌指蛋白251的片段（284-435残基）。 syntaxin结合蛋白1.我们使用酵母三杂交系统来确定这些betaII-C相互作用蛋白以及先前鉴定出的与非红系α血红蛋白（IP（alphaII-N）的四聚化区域相互作用的7种蛋白的作用s）[1]关于血影蛋白四聚体形成的结果表明，即使在存在alphaII-N的情况下，也有3个IP（betaII-C）能够结合betaII-C，并且有4个IP（alphaII-N）能够在存在betaII-C的情况下结合alphaII-N。我们还发现语法语法结合蛋白1片段废除了alphaII-N和betaII-C提示该蛋白可能抑制或调节非类红血球蛋白四聚体的形成。

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