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首页> 外文期刊>Biochemistry >Phage empty set 29 protein p6 is in a monomer-dimer equilibrium that shifts to higher association states at the millimolar concentrations found in vivo
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Phage empty set 29 protein p6 is in a monomer-dimer equilibrium that shifts to higher association states at the millimolar concentrations found in vivo

机译：噬菌体空集29蛋白p6处于单体二聚体平衡状态，在体内发现的毫摩尔浓度下会转变为更高的缔合态

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Protein p6 from Bacillus subtilis phage empty set29 (M-r = 11 800) binds in vitro to DNA forming a large nucleoprotein complex in which the :DNA wraps a multimeric protein core. The high intracellular abundance of protein p6 together with its ability to bind the whole empty set29 DNA in vitro strongly suggests that it plays a role in viral genome organization. We have determined by sedimentation equilibrium analysis that protein p6 (1-100 mu M range), in the absence of DNA, is in a monomer-dimer equilibrium, with an association constant (K-2) of similar to 2 x 10(5) M-1. The intracellular concentration of protein p6 (similar to 1 mM) was estimated measuring the number of copies per cell (7 x 10(5)) and the cell volume (1 x 10(-15) L), At concentrations around 1 mM, protein p6 associates into oligomers. This self-association behavior is compatible with a dimer-hexamer model (K-2,K-6 = 3.2 x 10(8) M-2) or with an isodesmic association of the dimer (K = 950 M-1), because the apparent weight-average molecular mass (M-w,M-a) does not reach saturation at the highest protein concentrations. The sedimentation coefficients of protein p6 monomer and dimer were 1.4 and 2.0, respectively, compatible with translational frictional ratios (f/f(0)) of 1.15 and 1.30, which slightly deviate from the hydrodynamics of a rigid globular protein. Taking together these results and considering the structure of the nucleoprotein complex, we speculate that the observed oligomers of protein p6 could mimic a scaffold on which DNA folds to form the nucleoprotein complex in vivo.
机译：枯草芽孢杆菌噬菌体空集29（M-r = 11800）的蛋白p6在体外与DNA结合，形成大的核蛋白复合物，其中：DNA包裹了多聚蛋白核心。蛋白p6的高细胞内丰度及其在体外结合整个空set29 DNA的能力强烈表明，它在病毒基因组的组织中发挥了作用。通过沉淀平衡分析，我们确定在不存在DNA的情况下，蛋白质p6（1-100μM范围）处于单体二聚体平衡中，缔合常数（K-2）近似于2 x 10（5） ）M-1。通过测量每个细胞的拷贝数（7 x 10（5））和细胞体积（1 x 10（-15）L）来估计蛋白p6的细胞内浓度（大约1 mM），蛋白p6缔合为寡聚物。这种自缔合行为与二聚六聚体模型（K-2，K-6 = 3.2 x 10（8）M-2）或与二聚体的等电势缔合（K = 950 M-1）兼容，因为表观重均分子量（Mw，Ma）在最高蛋白质浓度下未达到饱和。蛋白p6单体和二聚体的沉降系数分别为1.4和2.0，与1.15和1.30的平移摩擦比（f / f（0））兼容，这与刚性球状蛋白的流体动力学略有不同。综合这些结果并考虑核蛋白复合物的结构，我们推测观察到的蛋白p6寡聚体可以模拟一个支架，该支架上的DNA可以在体内折叠形成核蛋白复合物。

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