THE IDENTIFICATION AND CHARACTERIZATION OF AN ACTIN-BINDING SITE IN ALPHA-ACTININ BY MUTAGENESIS
THE IDENTIFICATION AND CHARACTERIZATION OF AN ACTIN-BINDING SITE IN ALPHA-ACTININ BY MUTAGENESIS
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DOI：
10.1016/0014-5793(92)80619-r
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发表时间：
1992-06-15
期刊：
影响因子：
3.5
通讯作者：
CRITCHLEY, DR
中科院分区：
文献类型：
--
作者：
KUHLMAN, PA;HEMMINGS, L;CRITCHLEY, DR
我们以前已经证明，α-肌动蛋白的N末端结合结构域在大肠杆菌中作为与谷胱甘肽-S转移酶的融合蛋白表达时仍然具有活性。在本研究中，我们在该结构域中进行了一系列N-端和C-端的缺失，并表明在120-134个残基中包含一个肌动蛋白结合位点。该区域内的氨基酸替换表明，几个高度保守的疏水残基参与了与F-肌动蛋白的结合。α-肌动蛋白和F-肌动蛋白之间的相互作用在本质上主要是疏水的，这一假设得到了结合相对独立于盐浓度的观察的支持。
We have shown previously that the N-terminal actin-binding domain of alpha-actinin retains activity when expressed in E. coli as a fusion protein with glutathione-S-transferase. In the present study we have made a series of N- and C-terminal deletions within this domain and show that an actin-binding site is contained within residues 120-134. Amino acid substitutions within this region indicate that several highly conserved hydrophobic residues are involved in binding to F-actin. The hypothesis that the interaction between alpha-actinin and F-actin is predominantly hydrophobic in nature is supported by the observation that binding is relatively independent of salt concentration.