Kuhlman P A, Hemmings L, Critchley D R
Department of Biochemistry, University of Leicester, UK.
FEBS Lett. 1992 Jun 15;304(2-3):201-6. doi: 10.1016/0014-5793(92)80619-r.
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.
我们之前已经表明，α-辅肌动蛋白的N端肌动蛋白结合结构域与谷胱甘肽-S-转移酶作为融合蛋白在大肠杆菌中表达时仍保留活性。在本研究中，我们对该结构域进行了一系列N端和C端缺失，并表明肌动蛋白结合位点包含在第120 - 134位残基内。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与F-肌动蛋白的结合。α-辅肌动蛋白与F-肌动蛋白之间的相互作用本质上主要是疏水性的这一假设，得到了结合相对独立于盐浓度这一观察结果的支持。
