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首页> 外文期刊>Journal of cell biology >Drosophila paramyosin/miniparamyosin gene products show a large diversity in quantity, localization, and isoform pattern: a possible role in muscle maturation and function.
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Drosophila paramyosin/miniparamyosin gene products show a large diversity in quantity, localization, and isoform pattern: a possible role in muscle maturation and function.

机译:果蝇副肌球蛋白/ miniparamyosin基因产物在数量,定位和同工型模式上显示出很大的多样性:可能在肌肉成熟和功能中起作用。

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The Drosophila paramyosin/miniparamyosin gene expresses two products of different molecular weight transcriptionally regulated from two different promoters. Distinct muscle types also have different relative amounts of myosin, paramyosin, and miniparamyosin, reflecting differences in the organization of their thick filaments. Immunofluorescence and EM data indicate that miniparamyosin is mainly located in the M line and at both ends of the thick filaments in Drosophila indirect flight muscles, while paramyosin is present all along the thick filaments. In the tergal depressor of the trochanter muscle, both proteins are distributed all along the A band. In contrast, in the waterbug, Lethocerus, both paramyosin and miniparamyosin are distributed along the length of the indirect flight and leg muscle thick filaments. Two-dimensional and one-dimensional Western blot analyses have revealed that miniparamyosin has several isoforms, focusing over a very wide pH range, all of which are phosphorylated in vivo. The changes in isoform patterns of miniparamyosin and paramyosin indicate a direct or indirect involvement of these proteins in muscle function and flight. This wide spectrum of potential regulatory characteristics underlines the key importance of paramyosin/miniparamyosin and its complex isoform pattern in the organization of the invertebrate thick filament.
机译:果蝇副肌球蛋白/小副肌球蛋白基因表达由两个不同启动子转录调控的不同分子量的两种产物。不同的肌肉类型还具有不同的肌球蛋白,副肌球蛋白和小副肌球蛋白的相对量,反映出粗丝组织的差异。免疫荧光和EM数据表明,小果蝇肌球蛋白主要位于M线和果蝇间接飞行肌肉的粗丝的两端,而副肌球蛋白一直存在于粗丝中。在转子肌的总压抑物中,两种蛋白质均沿A带分布。相反,在水生动物Lethocerus中,副肌球蛋白和小副肌球蛋白均沿间接飞行和腿部肌肉粗细丝的长度分布。二维和一维蛋白质印迹分析表明,小副肌球蛋白具有几种同工型,集中在非常宽的pH范围内,所有这些同工型均在体内被磷酸化。小型副肌球蛋白和副肌球蛋白同工型的变化表明这些蛋白直接或间接参与了肌肉功能和飞行。这种广泛的潜在调控特征强调了副肌球蛋白/小副肌球蛋白及其在无脊椎动物粗丝组织中的复杂同工型模式的关键重要性。

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