A mosaic multiple-binding model for the binding of caldesmon and myosin subfragment-1 to actin.
A mosaic multiple-binding model for the binding of caldesmon and myosin subfragment-1 to actin.
复制标题
卡尔德斯蒙和肌球蛋白亚片段 1 与肌动蛋白结合的镶嵌多重结合模型。
DOI：
10.1016/s0006-3495(92)81687-9
复制
发表时间：
1992
影响因子：
3.4
通讯作者：
Chalovich,JM
中科院分区：
文献类型：
--
作者：
Chen,YD;Chalovich,JM
Binding of caldesmon to actin causes a decrease in the quantity of bound myosin and results in a reduction in the rate of actin-activated adenosine triphosphate hydrolysis. It is generally assumed that the binding of caldesmon and myosin to actin is a pure competitive interaction. However, recent binding studies of enzyme digested caldesmon subfragments directed at mapping the actin binding site of caldesmon have shown that a small 8-kD fragment around the COOH-terminal can compete directly with the myosin subfragment 1 (S-1) binding to actin; at least one other fragment that binds to actin does not inhibit the actin-activated adenosine triphosphate activity of myosin. That is, only a part of the caldesmon sequence may be responsible for directly blocking the binding of S-1 to actin. This prompts us to question the actual mode of binding of intact caldesmon and myosin S-1 to actin: whether the entire intact caldesmon molecule is competing with S-1 binding (pure competitive model) or just a small part of it (mosaic multiple-binding model). To answer this question, we measured the amount of myosin S-1 and caldesmon bound per actin monomer as a function of the total concentration of S-1 added to the system at constant concentrations of actin and caldesmon. A formalism for calculating the titration data based on the pure competitive model and a mosaic multiple-binding model was then developed. When compared with theoretical calculations, it is found that the binding of caldesmon and S-1 to actin cannot be pure competitive if no cooperativity exists between S-1 and caldesmon.(ABSTRACT TRUNCATED AT 250 WORDS)
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期刊：
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DOI：
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发表时间：
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影响因子：
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