Influence of ionic strength, actin state, and caldesmon construct size on the number of actin monomers in a caldesmon binding site.

Fredricksen S; Cai A; Gafurov B; Resetar A; Chalovich JM

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Influence of ionic strength, actin state, and caldesmon construct size on the number of actin monomers in a caldesmon binding site.

机译：离子强度，肌动蛋白态和降钙胶质构建大小对肌蛋白粘结位点肌动蛋白单体数量的影响。

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There is no consensus on the mechanism of inhibition of actin-myosin ATPase activity by caldesmon. Various models are based on different assumptions for the number of actin monomers that constitute a caldesmon binding site. Differences in binding behavior may be due to variations in the assay, the range of caldesmon concentrations, the type of caldesmon, and the method of data analysis used. We have evaluated these factors by measuring binding in the presence and absence of tropomyosin with both intact caldesmon and a recombinant 35 kDa actin binding fragment and with actin initially in the polymerized state or monomeric state. In all cases caldesmon binding could be simulated with a model having one class of binding sites. However, the number of actin monomers constituting a site was variable. Binding to F-actin at 165 mM ionic strength was best described with 7 actin monomers per site. When caldesmon bound to actin during the polymerization of G-actin, the size of the binding site was 3. Binding of the expressed truncated fragment, Cad35, could be described with 3 monomers per site. A simple interpretation of the data is that caldesmon binds tightly to 2-3 actin monomers. Additional parts of caldesmon bind less tightly to actin, causing caldesmon to cover approximately 7 actin monomers. The appendix contains an analysis of several binding curves with multiple binding site models. There is no compelling evidence for two classes of binding sites.

机译：对Caldesmon抑制肌动蛋白 - 肌球蛋白ATP酶活性的机制没有共识。各种模型基于构成Caldesmon结合位点的肌动蛋白单体数量的不同假设。结合行为的差异可能是由于测定的变化，Caldesmon浓度，Caldesmon的类型和使用的数据分析方法。我们通过用完整的钙钠和重组35kDa肌动蛋白结合片段测量了对Gropomyosin的存在和不存在的结合来评估这些因素，并且最初以聚合状态或单体状态致动肌蛋白。在所有情况下，可以用具有一类结合位点的模型模拟Caldesmon结合。然而，构成位点的肌动蛋白单体的数量是可变的。每位位点7次肌动蛋白单体最好地描述于165mM离子强度的与F-肌动蛋白的结合。当在G-actin的聚合过程中致肌蛋白的抗粘接剂时，结合位点的尺寸为3.表达截短的片段CAD35的结合可以用每位位点3个单体描述。对数据的简单解释是Caldesmon紧密结合到2-3个肌动蛋白单体。另外的Caldesmon的零件粘合得很紧密，肌动蛋白，导致Caldesmon覆盖大约7种肌动蛋白单体。附录包含具有多个绑定站点模型的几种绑定曲线的分析。两种绑定站点没有令人信服的证据。

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来源
《Biochemistry》 |2003年第20期|共13页
作者
Fredricksen S; Cai A; Gafurov B; Resetar A; Chalovich JM;
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作者单位

Department of Biochemistry and Molecular Biology The Brody School of Medicine at East Carolina University 600 Moye Boulevard Greenville North Carolina 27858-4354.;

Station de Recherches sur la Viande Institut National de la Recherche Agronomique Theix 63122 Saint-Genes Champanelle;

Station de Recherches sur la Viande Institut National de la Recherche Agronomique Theix 63122 Saint-Genes Champanelle;

Station de Recherches sur la Viande Institut National de la Recherche Agronomique Theix 63122 Saint-Genes Champanelle;

Station de Recherches sur la Viande Institut National de la Recherche Agronomique Theix 63122 Saint-Genes Champanelle;

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正文语种 eng
中图分类生物化学;
关键词
Actins; Caldesmon; binding; Binding Sites; SIZES; 肌动蛋白类; 结合部位;

机译：Actins;Caldesmon;binding;Binding Sites;SIZES;肌动蛋白类;结合部位;

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专利

1. Influence of ionic strength, actin state, and caldesmon construct size on the number of actin monomers in a caldesmon binding site. [J] . Fredricksen S, Cai A, Gafurov B, Biochemistry . 2003,第20期

机译：离子强度，肌动蛋白态和降钙胶质构建大小对肌蛋白粘结位点肌动蛋白单体数量的影响。
2. Both N-terminal myosin-binding and C-terminal actin-binding sites on smooth muscle caldesmon are required for caldesmon- mediated inhibition of actin filament velocity [J] . Ze Wang, He Jiang, Zhi-Qiong Yang Proceedings of the National Academy of Sciences of the United States of America . 1997,第22期

机译：肌钙蛋白介导的肌动蛋白丝速度的抑制作用需要平滑肌caldesmon上的N端肌球蛋白结合位点和C端肌动蛋白结合位点
3. The binding of distinct segments of actin to multiple sites in the C-terminus of caldesmon: comparative aspects of actin interaction with troponin-I and caldesmon. [J] . Mornet D, Bonet Kerrache A, Strasburg GM, Biochemistry . 1995,第6期

机译：肌动蛋白的不同节段与caldesmon C末端的多个位点的结合：肌动蛋白与肌钙蛋白I和caldesmon相互作用的比较方面。
4. Influence of the N Terminus and the Actin-Binding Motif of Thymosin β_4 on Its Interaction with G-Actin [C] . ROBERT E. ZOUBEK, EWALD HANNAPPEL International Symposiumn on Thymosins in Health and Disease; 20070321-24; Washington,DC(US) . 2007

机译：胸腺素β_4的N末端和肌动蛋白结合基序对其与G-肌动蛋白相互作用的影响
5. Development and characterization of a polymerization deficient actin monomer and longitudinal actin dimer. [D] . Loncar, Ana. 2010

机译：聚合缺陷型肌动蛋白单体和纵向肌动蛋白二聚体的开发和表征。
6. Parallel inhibition of active force and relaxed fiber stiffness by caldesmon fragments at physiological ionic strength and temperature conditions: additional evidence that weak cross-bridge binding to actin is an essential intermediate for force generation. [O] . T Kraft, J M Chalovich, L C Yu, 1995

机译：Caldesmon片段在生理离子强度和温度条件下同时抑制活性力和松弛的纤维硬度：额外的证据表明与肌动蛋白的弱横桥结合是产生力的必要中间体。
7. Parallel inhibition of active force and relaxed fiber stiffness by caldesmon fragments at physiological ionic strength and temperature conditions: additional evidence that weak cross-bridge binding to actin is an essential intermediate for force generation [O] . Kraft, T., Chalovich, J. M., Yu, L. C., 1995

机译：Caldesmon片段在生理离子强度和温度条件下同时抑制活性力和松弛的纤维刚度：额外的证据表明与肌动蛋白的弱横桥结合是产生力的必要中间

Influence of ionic strength, actin state, and caldesmon construct size on the number of actin monomers in a caldesmon binding site.

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