Unidad de Biofísica (CSIC-UPV/EHU), and Departamento de Bioquímica y BiologíaMolecular (UPV/EHU), Facultad de Ciencia y Tecnología, Universidad del País Vasco, P.O. Box 644, Bilbao, Spain.
FEBS Lett. 2010 Mar 5;584(5):929-34. doi: 10.1016/j.febslet.2010.01.029. Epub 2010 Jan 19.
ClpB is a member of the AAA+ superfamily that forms a ring-shaped homohexamer. Each protomer contains two nucleotide binding domains arranged in two rings that hydrolyze ATP. We extend here previous studies on ClpB nucleotide utilization requirements by using an experimental approach that maximizes random incorporation of different subunits into the protein hexamer. Incorporation of one subunit unable to bind or hydrolyze ATP knocks down the chaperone activity, while the wt hexamer can accommodate two mutant subunits that hydrolyze ATP in only one protein ring. Four subunits seem to build the functional cooperative unit, provided that one of the protein rings contains active nucleotide binding sites.
ClpB 是 AAA+ 超家族的成员，形成环形同六聚体。每个单体包含两个核苷酸结合结构域，排列在两个环中，水解 ATP。我们通过使用一种实验方法扩展了之前关于 ClpB 核苷酸利用要求的研究，该方法最大限度地增加了不同亚基随机掺入蛋白质六聚体的情况。掺入一个无法结合或水解 ATP 的亚基会降低伴侣活性，而 wt 六聚体可以容纳两个仅在一个蛋白质环中水解 ATP 的突变亚基。四个亚基似乎构建了功能协同单位，前提是其中一个蛋白质环包含活性核苷酸结合位点。
