• 主题
高级搜索  >
历史搜索 清空历史
首页> 美国卫生研究院文献>Genetics >The Biologically Relevant Targets and Binding Affinity Requirements for the Function of the Yeast Actin-Binding Protein 1 Src-Homology 3 Domain Vary With Genetic Context
【2h】

The Biologically Relevant Targets and Binding Affinity Requirements for the Function of the Yeast Actin-Binding Protein 1 Src-Homology 3 Domain Vary With Genetic Context

机译：酵母肌动蛋白结合蛋白1 Src同源3域的功能与遗传背景有关的生物学相关目标和结合亲和力要求。

代理获取
本网站仅为用户提供外文OA文献查询和代理获取服务，本网站没有原文。下单后我们将采用程序或人工为您竭诚获取高质量的原文，但由于OA文献来源多样且变更频繁，仍可能出现获取不到、文献不完整或与标题不符等情况，如果获取不到我们将提供退款服务。请知悉。
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Many protein–protein interaction domains bind to multiple targets. However, little is known about how the interactions of a single domain with many proteins are controlled and modulated under varying cellular conditions. In this study, we investigated the in vivo effects of Abp1p SH3 domain mutants that incrementally reduce target-binding affinity in four different yeast mutant backgrounds in which Abp1p activity is essential for growth. Although the severity of the phenotypic defects observed generally increased as binding affinity was reduced, some genetic backgrounds (prk1Δ and sla1Δ) tolerated large affinity reductions while others (sac6Δ and sla2Δ) were much more sensitive to these reductions. To elucidate the mechanisms behind these observations, we determined that Ark1p is the most important Abp1p SH3 domain interactor in prk1Δ cells, but that interactions with multiple targets, including Ark1p and Scp1p, are required in the sac6Δ background. We establish that the Abp1p SH3 domain makes different, functionally important interactions under different genetic conditions, and these changes in function are reflected by changes in the binding affinity requirement of the domain. These data provide the first evidence of biological relevance for any Abp1p SH3 domain-mediated interaction. We also find that considerable reductions in binding affinity are tolerated by the cell with little effect on growth rate, even when the actin cytoskeletal morphology is significantly perturbed.
机译：许多蛋白质间相互作用域与多个靶标结合。然而，关于如何在变化的细胞条件下控制和调节单个结构域与许多蛋白质的相互作用知之甚少。在这项研究中，我们调查了Abp1p SH3结构域突变体的体内效应，该突变体在四个不同的酵母突变体背景下（其中Abp1p活性对于生长至关重要）逐渐降低了靶标结合亲和力。尽管观察到的表型缺陷的严重程度通常随着结合亲和力的降低而增加，但某些遗传背景（prk1Δ和sla1Δ）可以忍受较大的亲和力降低，而其他遗传背景（sac6Δ和sla2Δ）对这些降低更为敏感。为了阐明这些观察结果背后的机制，我们确定Ark1p是prk1Δ细胞中最重要的Abp1p SH3域相互作用子，但在sac6Δ背景中需要与多个靶标（包括Ark1p和Scp1p）相互作用。我们建立了Abp1p SH3结构域在不同的遗传条件下进行了不同的，功能上重要的相互作用，并且功能的这些变化通过该结构域的结合亲和力要求的变化反映出来。这些数据为任何Abp1p SH3域介导的相互作用的生物学相关性提供了第一个证据。我们还发现，即使肌动蛋白的细胞骨架形态受到显着扰动，细胞对结合亲和力的显着降低却几乎没有影响。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
代理获取

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号