ARTHRIN, A MYOFIBRILLAR PROTEIN OF INSECT FLIGHT-MUSCLE, IS AN ACTIN UBIQUITIN CONJUGATE
ARTHRIN, A MYOFIBRILLAR PROTEIN OF INSECT FLIGHT-MUSCLE, IS AN ACTIN UBIQUITIN CONJUGATE
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DOI：
10.1016/0092-8674(87)90149-8
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发表时间：
1987-10-23
期刊：
影响因子：
64.5
通讯作者：
FYRBERG, EA
中科院分区：
文献类型：
--
作者：
BALL, E;KARLIK, CC;FYRBERG, EA
一些昆虫的飞行肌含有一种称为arthrin的肌原纤维蛋白，它与肌动蛋白（分子量43，000）密切相关。在这里，我们证明了arthrin（分子量55，000）是泛素化的肌动蛋白。我们表明，在Act 88 FM 342（一种不能飞的果蝇突变体，其中Act 88 F肌动蛋白基因指定glu 93 → lys置换）中，肌动蛋白III和青蒿素的等电点都发生了移动，表明两者都由相同的基因编码。青蒿素与抗泛素抗体反应，这表明其额外质量是由泛素连接引起的。大约七分之一的肌原纤维肌动蛋白是稳定的泛素化，这表明可能有一个arthrin分子每个肌动蛋白-原肌球蛋白-肌钙蛋白合作单位。Arthin的形成滞后于肌动蛋白III的形成几个小时，这意味着泛素化与肌原纤维组装的某些方面相吻合。
Flight muscles of some insects contain a myofibrillar protein termed arthrin, which is closely related to actin (mw 43,000). Here we demonstrate that arthrin (mw 55,000) is ubiquitinated actin. We show that in Act88FM342, a flightless Drosophila mutant wherein the Act88F actin gene specifies a glu93.fwdarw.lys replacement, isoelectric points of both actin III and arthrin are shifted, revealing that both are encoded by the same gene. Arthrin reacts with an anti-ubiquitin antibody, which demonstrates that its extra mass results from ubiquitin ligation. Approximately one-seventh of myofibrillar actin is stably ubiquitinated, suggesting that there may be one arthrin molecule per actin-tropomyosin-troponin cooperative unit. Arthin formation lags several hours behind that of actin III, implying that ubiquitination coincides with some aspect of myofibril assembly.