Myosin heavy chain genes expressed in juvenile and adult silver carp Hypopthalmichthys molitrix: Novel fast-type myosin heavy chain genes of silver carp
Myosin heavy chain genes expressed in juvenile and adult silver carp Hypopthalmichthys molitrix: Novel fast-type myosin heavy chain genes of silver carp
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DOI：
10.1016/j.gene.2008.11.022
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发表时间：
2009-03-01
期刊：
影响因子：
3.5
通讯作者：
Watabe, Shugo
中科院分区：
文献类型：
--
作者：
Fukushima, Hideto;Ikeda, Daisuke;Watabe, Shugo
银鱼是一种温带温带鱼类，其肌肉被认为在生长的不同阶段表达多种类型的肌球蛋白重链(MYH)基因，并对环境温度进行调整。本研究对幼鱼和成鱼肌肉中MYH基因的表达进行了研究。采用RACE策略，利用一组FAST类型的MYH特异引物，从成鱼快速骨骼肌构建的文库中分离到5种类型的MYH基因克隆，分别命名为scMYH(F1)、scMYH(F2)、scMYH(F3)、scMYH(F4)和scMYH(F5)。ScMYH(F1)、scMYH(F3)和scMYH(F5)与分别在30、10和20℃驯化的草鱼快速骨骼肌中表达的gcMYH(F30)、gcMYH(F10)和gcMYH(F1)的核苷酸序列同源性分别为96%、98%和96%。ScMYH(F2)和scMYH(F4)与鳕鱼慢骨骼肌中的A4型MYH有较高的同源性。系统发育分析表明，scMYH(F1)和scMYH(F5)与鱼类成体快型MYH同源，scMYH(F2)和scMYH(F4)与鱼类慢型快型MYH聚为一类，scMYH(F3)与鱼胚胎快型MYH同源。有趣的是，无论驯化温度为10℃、18℃或26℃，鲤鱼幼鱼都主要表达scMYH(F3)。比较推导的氨基酸序列中scMYH(F1)、scMYH(F2)和scMYH(F3)的氨基酸序列，推测肌球蛋白亚段1(S1)中的ATP、肌动蛋白和必需和调节轻链的结合部位彼此之间有很高的同源性(81%-100%)。然而，它们在S1中的loop-1和loop-2区域是高度可变的，这表明它们的功能不同。肌球蛋白亚段-2和L-肌球蛋白的氨基酸序列在上述3个scMYH中具有较高的同源性，分别为90-91%和86-90%。(C)2008爱思唯尔B.V.保留所有权利。
Silver carp Hypopthalmichthys molitrix is eurythermal temperate fish, whose muscle is considered to express several types of myosin heavy chain (MYH) genes at different stages of its growth and to adjust to the environmental temperature. In this study, MYH genes expressed in the muscles of juvenile and adult silver carp were investigated. Five types of MYH cDNA clone were isolated from silver carp (H. molitrix) by RACE strategy using a set of fast-type MYH specific primers, and termed scMYH(F1), scMYH(F2), scMYH(F3), scMYH(F4) and scMYH(F5) in the order of their abundance in cDNA libraries constructed from fast skeletal muscles of adult silver carp. scMYH(F1), scMYH(F3) and scMYH(F5) showed high nucleotide sequence identities of 96, 98 and 96% to gcMYH(F30), gcMYH(F10) and gcMYH(F1), respectively, that encode MYHs predominantly expressed in fast skeletal muscle of grass carp (Ctenopharyngodon idella) acclimated to 30, 10 and 20 degrees C, respectively. scMYH(F2) and scMYH(F4) showed a high identity to A4-type MYH from rock cod (Notothenia coriiceps) slow skeletal muscle. Phylogenetic analysis demonstrated that scMYH(F1), and scMYH(F5) were monophyletic with fish adult fast-type MYHs, whereas scMYH(F2) and scMYH(F4) formed a cluster with fish slow-like fast-type MYH, and scMYH(F3) did with fish embryonic fast-type MYHs. Interestingly, juvenile silver carp predominantly expressed scMYH(F3) irrespective of acclimation temperatures at 10, 18 or 26 degrees C. The comparison among scMYH(F1), scMYH(F2) and scMYH(F3) in the deduced amino acid sequence revealed that the putative binding sites for ATP, actin, and essential and regulatory light chains in myosin subfragment-1 (S1) have high identities with each other (81-100%). However, their loop-1 and loop-2 regions in S1 were highly variable, suggesting their different functions. The deduced amino acid sequences of myosin subfragment-2 and L-meromyosin showed high identities of 90-91% and 86-90%, respectively, among the above three scMYHs. (c) 2008 Elsevier B.V. All rights reserved.