Characterization of MR-1, a novel Myofibrillogenesis regulator in human muscle
Characterization of MR-1, a novel Myofibrillogenesis regulator in human muscle
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DOI：
10.1093/abbs/36.6.412
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发表时间：
2004-06-01
影响因子：
3.7
通讯作者：
Gong, LM
中科院分区：
文献类型：
--
作者：
Li, TB;Liu, XH;Gong, LM
肌动蛋白-肌球蛋白收缩器由几种粗丝和细丝蛋白组成。在这个高度有序的过程中涉及特定的调节机制。在本文中，我们报告了一种新的肌原纤维生成调节剂，MR-1的鉴定和表征。采用EST数据库搜索、PCR和RACE相结合的策略，从人骨骼肌cDNA文库中克隆了MR-1基因。MR-1]基因位于人染色体2 q35上，编码一个142个氨基酸的蛋白质。北方杂交结果显示，MR-1在骨骼肌中的表达量最高，在心脏、肝脏和肾脏中也有一定水平的表达。免疫组化证实MR-1蛋白存在于人心肌肌原纤维中。通过酵母双杂交筛选和体外结合实验证实MR-1可以与肌球蛋白调节轻链（myosin regulatory light chain）、肌桥蛋白I（myomesin I）和β-烯醇化酶（beta-enolase）等肌节蛋白相互作用。这些研究提示MR-1可能在肌细胞中起调节作用，值得进一步研究。
The actin-myosin contractile apparatus consists of several thick filament and thin filament proteins. Specific regulatory mechanisms are involved in this highly ordered process. In this paper, we reported the identification and characterization of a novel myofibrillogenesis regulator, MR-1. The MR-1 gene was cloned from human skeletal muscle cDNA library by using a strategy that involves EST data base searching, PCR and RACE. The MR-1] gene is located on human chromosome 2q35 and encodes a 142 aa protein. Northern blot revealed that the mRNA level of MR-1 was highest in the skeletal muscle and certain level of MR-1 expression was also observed in heart, liver and kidney. Immunohistochemical assay confirmed that the MR-1 protein existed in human myocardial myofibrils. It was found by yeast two-hybrid screening and confirmed by in vitro binding assay that MR-1 could interact with sarcomeric proteins, such as myosin regulatory light chain, myomesin I and beta-enolase. These studies suggested that MR-1 might play,a regulatory role in the muscle cell and it was worth investigating further.