ATP-mediated changes in cross-subunit interactions in the RecA protein.
ATP-mediated changes in cross-subunit interactions in the RecA protein.
复制标题
ATP 介导的 RecA 蛋白跨亚基相互作用的变化。
DOI：
10.1021/bi011081u
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发表时间：
2001
期刊：
影响因子：
2.9
通讯作者：
Knight,KL
中科院分区：
文献类型：
--
作者：
Logan,KM;Forget,AL;Verderese,JP;Knight,KL
RecA蛋白经历了ATP和DNA诱导的构象变化，导致游离蛋白细丝的螺旋参数与RecA/ATP/DNA核蛋白细丝的螺旋参数不同。先前对RecA寡聚体界面特定区域的突变研究表明，由残基K6和R28形成的跨亚单位接触对于游离蛋白质低聚体的稳定比核蛋白细丝更重要[Eldin，S.，等人。(2000)J.Mol.比奥尔。299、91−101]。使用带有特殊设计的半胱氨酸取代的突变蛋白，我们在这里表明，在ATP或ATP/DNA存在的情况下，该区域某些位置的交叉亚单位二硫键形成的效率会发生变化。我们的结果支持这样的观点，即在游离RecA蛋白和RecA/ATP/DNA核蛋白细丝中，发生在亚基界面这一区域内的特定跨亚单位相互作用是不同的。
RecA protein undergoes ATP- and DNA-induced conformational changes that result in different helical parameters for free protein filaments versus RecA/ATP/DNA nucleoprotein filaments. Previous mutational studies of a particular region of the RecA oligomeric interface suggested that cross-subunit contacts made by residues K6 and R28 were more important for stabilization of free protein oligomers than nucleoprotein filaments [Eldin, S., et al. (2000)J. Mol. Biol. 299, 91−101]. Using mutant proteins with specifically engineered Cys substitutions, we show here that the efficiency of cross-subunit disulfide bond formation at certain positions in this region changes in the presence of ATP or ATP/DNA. Our results support the idea that specific cross-subunit interactions that occur within this region of the subunit interface are different in free RecA protein versus RecA/ATP/DNA nucleoprotein filaments.