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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >The functional domains of human ventricular myosin light chain 1
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The functional domains of human ventricular myosin light chain 1

机译：人心室肌球蛋白轻链1的功能域

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The biological functions of the myosin light chain 1 (LC1) have not been clearly elucidated yet. In this work we cloned and expressed N- and C- terminal fragments of human ventricular LC1 (HVLC1) containing amino acid residues 1-98 and 99-195 and two parts, NN and NC of N fragment in GST-fusion forms, respectively. Using GST pull-down assay, the direct binding experiments of LC1 with rat cardiac G-actin, F-actin and thin filaments, as well as rat cardiac myosin heavy chain (RCMHC) have been performed. Furthermore, the recombinant complexes of rat myosin S I with N- and C-fragments, as well as the whole molecular of HVLC1 were generated. The results suggested that both binding sites of HVLC1 for actin and myosin heavy chain are positioned in its N-terminal fragment, which may contain several actin-binding sites in tandem. The polymerization of G-actin, the tropomyosin and troponin molecules located in the thin filaments do not hinder the binding of N-terminal fragment of HVLC1 with actin and thin filaments in vitro. The recombinant complex of rat cardiac myosin S1 (RCMS1) with N fragment of HVLC1 greatly decreased actin-actived Mg2+-ATPase activity for lack of C fragment. We conclude that the N-fragment is the binding domain of human ventricular LC1, whereas the C-fragment serves as a functional domain, which may be more involved in the modulation of the actin-activated ATPase activity of myosin. (C) 2003 Elsevier Science B.V. All rights reserved. [References: 32]
机译：肌球蛋白轻链1（LC1）的生物学功能尚未明确阐明。在这项工作中，我们克隆并表达了人心室LC1（HVLC1）的N端和C端片段，分别包含GST融合形式的氨基酸残基1-98和99-195以及N片段的NN和NC两部分。使用GST下拉测定法，已进行LC1与大鼠心脏G-肌动蛋白，F-肌动蛋白和细丝以及大鼠心脏肌球蛋白重链（RCMHC）的直接结合实验。此外，还产生了大鼠肌球蛋白S I与N和C片段的重组复合物，以及HVLC1的整个分子。结果表明，HVLC1与肌动蛋白和肌球蛋白重链的结合位点均位于其N端片段中，该片段可能串联包含多个肌动蛋白结合位点。位于细丝中的G-肌动蛋白，原肌球蛋白和肌钙蛋白分子的聚合在体外不会阻碍HVLC1的N末端片段与肌动蛋白和细丝的结合。大鼠心肌肌球蛋白S1（RCMS1）与HVLC1的N片段的重组复合物大大降低了肌动蛋白激活的Mg2 + -ATPase活性，缺乏C片段。我们得出的结论是，N片段是人心室LC1的结合域，而C片段则是一个功能域，它可能更多地参与肌球蛋白肌动蛋白激活的ATPase活性的调节。 （C）2003 Elsevier Science B.V.保留所有权利。 [参考：32]

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