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首页> 外文期刊>Cell motility and the cytoskeleton >Native nonmuscle myosin II stability and light chain binding in Drosophila melanogaster.
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Native nonmuscle myosin II stability and light chain binding in Drosophila melanogaster.

机译：果蝇的天然非肌肉肌球蛋白II稳定性和轻链结合。

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Native nonmuscle myosin IIs play essential roles in cellular and developmental processes throughout phylogeny. Individual motor molecules consist of a heterohexameric complex of three polypeptides which, when properly assembled, are capable of force generation. Here, we more completely characterize the properties, relationships and associations that each subunit has with one another in Drosophila melanogaster. All three native nonmuscle myosin II polypeptide subunits are expressed in close to constant stoichiometry to each other throughout development. We find that the stability of two subunits, the heavy chain and the regulatory light chain, depend on one another whereas the stability of the third subunit, the essential light chain, does not depend on either the heavy chain or regulatory light chain. We demonstrate that heavy chain aggregates, which form when regulatory light chain is lacking, associate with the essential light chain in vivo-thus showing that regulatory light chain association is required for heavy chain solubility. By immunodepletion we find that the majority of both light chains are associated with the nonmuscle myosin II heavy chain but pools of free light chain and/or light chain bound to other proteins are present. We identify four myosins (myosin II, myosin V, myosin VI and myosin VIIA) and a microtubule-associated protein (asp/Abnormal spindle) as binding partners for the essential light chain (but not the regulatory light chain) through mass spectrometry and co-precipitation. Using an in silico approach we identify six previously uncharacterized genes that contain IQ-motifs and may be essential light chain binding partners.
机译：天然非肌肉肌球蛋白IIs在整个系统发育过程中都在细胞和发育过程中发挥重要作用。单个马达分子由三个多肽的异六聚体复合物组成，当正确组装时，它们能够产生力。在这里，我们更完整地描述了果蝇中每个亚基彼此之间的特性，关系和关联。在整个发育过程中，所有三个天然的非肌肉肌球蛋白II多肽亚基都以恒定的化学计量表达。我们发现，两个亚基，重链和调节性轻链的稳定性相互依赖，而第三亚基，必需的轻链，的稳定性不依赖重链或调节性轻链。我们证明当缺乏调节性轻链时形成的重链聚集体与体内必需的轻链缔合，因此表明调节性轻链缔合对于重链溶解度是必需的。通过免疫耗竭，我们发现两条轻链中的大多数都与非肌肉肌球蛋白II重链相关，但是存在与其他蛋白质结合的自由轻链和/或轻链库。我们通过质谱法和质谱法鉴定了四种肌球蛋白（肌球蛋白II，肌球蛋白V，肌球蛋白VI和肌球蛋白VIIA）和微管相关蛋白（asp /异常纺锤体）作为必需轻链（而非调节性轻链）的结合伴侣。 -沉淀。使用计算机方法，我们确定了六个以前未表征的基因，这些基因含有IQ基序，可能是必不可少的轻链结合伴侣。

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