Nucleotide‐dependent oligomerization of C1pB from Escherichia coli
Nucleotide‐dependent oligomerization of C1pB from Escherichia coli
复制标题
大肠杆菌 C1pB 的核苷酸依赖性寡聚反应
作者：
M. Żółkiewski;M. Kessel;A. Ginsburg;M. Maurizi
ClpB（95-和80-kDa亚基的混合物）的自缔合已经用凝胶过滤色谱，分析超离心和电子显微镜进行了研究。单体ClpB在低蛋白浓度（0.07 mg/mL）下占优势，而寡聚形式在>4 mg/mL下高度聚集。在2 mM ATP或腺苷5′-O-硫代三磷酸（ATPγS）存在下，寡聚体形成增强。相反，2 mMADP抑制ClpB的完全寡聚化。通过凝胶过滤、沉降速度和电子显微镜图像平均法测定的ATP-或ATPγS-诱导的寡聚体的表观大小以及通过沉降平衡测定的分子量与ClpB六聚体的表观大小一致。这些结果表明ClpB的寡聚化反应与其他Hsp 100蛋白的寡聚化反应相似。
Self‐association of ClpB (a mixture of 95‐ and 80‐kDa subunits) has been studied with gel filtration chromatography, analytical ultracentrifugation, and electron microscopy. Monomeric ClpB predominates at low protein concentration (0.07 mg0mL), while an oligomeric form is highly populated at >4 mg/mL. The oligomer formation is enhanced in the presence of 2 mM ATP or adenosine 5′‐O‐thiotriphosphate (ATPγS). In contrast, 2 mMADP inhibits full oligomerization of ClpB. The apparent size of the ATP‐ or ATPγS‐induced oligomer, as determined by gel filtration, sedimentation velocity and electron microscopy image averaging, and the molecular weight, as determined by sedimentation equilibrium, are consistent with those of a ClpB hexamer. These results indicate that the oligomerization reactions of ClpB are similar to those of other Hsp100 proteins.
DOI：
10.1016/s0021-9258(17)41804-7
发表时间：
1994-02
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
D. Parsell;A. Kowal;S. Lindquist
通讯作者：
D. Parsell;A. Kowal;S. Lindquist
影响因子：
2.9
作者：
STAFFORD, WF
通讯作者：
STAFFORD, WF