大肠杆菌细胞质膜上的GroEL与SecA的靶向作用。
Targeting of GroEL to SecA on the cytoplasmic membrane of Escherichia coli.
作者信息
Bochkareva E S, Solovieva M E, Girshovich A S
机构信息
Department of Biological Chemistry, Weizmann Institute of Science, Rehovot, Israel.
出版信息
Proc Natl Acad Sci U S A. 1998 Jan 20;95(2):478-83. doi: 10.1073/pnas.95.2.478.
Abstract
Chaperonin GroEL has been found to interact with isolated cytoplasmic membrane of Escherichia coli. Interaction requires Mg ions, whereas MgATP inhibits, and inhibition is stronger in the presence of co-chaperonin GroES. "Heat-shock" of the membrane at 45 degrees C destroys irreversibly its ability to bind GroEL. The binding of GroEL is characterized by saturation with a maximum of about 100 pmol GroEL bound per mg of total membrane protein, indicating a limited capacity and specificity of the membrane to bind GroEL. According to results of immunoblotting analysis and cleavable photoactivable cross-linking, a membrane target of GroEL is SecA, a protein known as a central component of the translocation machinery. Moreover, in some cases GroEL could modulate a cycle of association of SecA with the membrane by stimulating release of SecA from the membrane. A physiological role of targeting of GroEL in or close to the protein-conducting membrane apparatus is discussed.
摘要
伴侣蛋白GroEL已被发现可与大肠杆菌分离的细胞质膜相互作用。这种相互作用需要镁离子，而MgATP则起抑制作用，并且在有共伴侣蛋白GroES存在时抑制作用更强。在45摄氏度对膜进行“热休克”会不可逆地破坏其结合GroEL的能力。GroEL的结合具有饱和性，每毫克总膜蛋白最多结合约100皮摩尔GroEL，这表明膜结合GroEL的能力和特异性有限。根据免疫印迹分析和可切割的光活化交联结果，GroEL的一个膜靶点是SecA，一种已知为转运机制核心成分的蛋白质。此外，在某些情况下，GroEL可通过刺激SecA从膜上释放来调节SecA与膜的结合循环。本文讨论了GroEL靶向蛋白质传导膜装置内部或附近的生理作用。
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