Structural differences in the crossbridge head of temperature-associated myosin subfragment-1 isoforms from carp fast skeletal muscle.
Structural differences in the crossbridge head of temperature-associated myosin subfragment-1 isoforms from carp fast skeletal muscle.
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鲤鱼快速骨骼肌与温度相关的肌球蛋白亚片段 1 亚型的横桥头的结构差异。
DOI：
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复制
发表时间：
1997
期刊：
影响因子：
--
通讯作者：
S. Watabe
中科院分区：
文献类型：
--
作者：
Y. Hirayama;S. Watabe
我们确定了热驯化鲤鱼快骨骼肌肌球蛋白亚片段-1重链的三个与驯化温度相关的亚型的主要结构。这些异构体是通过延长在10℃和30℃驯化的鲤鱼中表达的编码肌球蛋白重链棒部分的cdna的5'-区域，以及编码中间结构的区域克隆出来的[Imai， J. Hirayama， Y., Kikuchi， K., Kakinuma， M. & Watabe， S. (1997) J. Exp. biological, 200,27 -34]。这三个亚型在一级结构上基本相似，10°C型和中间型、10°C型和30°C型、中间和30°C型肌球蛋白重链的相似度分别为94.8%、90.9%和92%。然而，从n端开始的前60个氨基酸残基中，在10°C和30°C型重链中，可以清楚地观察到同种异构体的特异性差异，其中中间型在其序列中显示出与10°C和30°C型同种异构体相比的中间特征。在10°C和30°C型异构体之间的两个表面环中观察到其他显著差异。16个氨基酸残基中有5个在靠近atp结合袋的环1中有不同，20个氨基酸残基中有6个在肌动蛋白结合位点的环2中有不同。已知环绕atp结合袋的连接β -片的环在三种类型的初级结构中高度保守。northern blot结果显示，10℃和20℃环境下10℃和中间型异构体的mRNA积累量显著高于30℃环境，30℃环境下30℃环境下30℃C型异构体的mRNA积累量显著高于10℃和20℃环境。
We determined the primary structures of the three acclimation-temperature-associated isoforms of myosin subfragment-1 heavy chain from fast skeletal muscle of thermally acclimated carp. These isoforms were cloned by extending 5'-regions of cDNAs that encode the rod part of myosin heavy chain specifically expressed in 10 degrees C- and 30 degrees C-acclimated carp, together with the region that encodes an intermediate structure [Imai, J., Hirayama, Y., Kikuchi, K., Kakinuma, M. & Watabe, S. (1997) J. Exp. Biol. 200, 27-34]. These three isoforms generally resembled each other in primary structure, showing 94.8, 90.9, and 92% similarity between the 10 degrees C- and intermediate-type, between the 10 degrees C- and 30 degrees C-type, and between the intermediate- and 30 degrees C-type myosin heavy chains, respectively. However, isoform-specific differences were clearly observed between the 10 degrees C- and 30 degrees C-type heavy chains in the first 60 amino acid residues from the N-terminus, where the intermediate-type showed an intermediate feature in its sequence compared to the 10 degrees C- and 30 degrees C-type isoforms. Other striking differences were observed in two surface loops between the 10 degrees C- and 30 degrees C-type isoform. Five amino acid residues out of sixteen were different in loop 1 near the ATP-binding pocket, and six out of twenty were different in loop 2 on the actin-binding site. The loops connecting beta-sheets that are known to surround the ATP-binding pocket were highly conserved in primary structure for the three types. In northern blot analysis, the accumulated mRNA levels of the 10 degrees C- and intermediate-type isoforms were significantly higher in carp acclimated to 10 degrees C and 20 degrees C than carp acclimated to 30 degrees C, whereas the level of the 30 degrees C-type isoform was significantly higher in carp acclimated to 30 degrees C than those acclimated to 10 degrees C and 20 degrees C.
肌球蛋白亚片段 1 与 F-肌动蛋白的结合。
DOI：
10.1016/0006-291x(92)92354-z
发表时间：
1992
影响因子：
3.1
作者：
Andreev,O;Borejdo,J
通讯作者：
Borejdo,J
运动蛋白2：肌球蛋白。
DOI：
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发表时间：
1995
期刊：
Protein profile.
影响因子：
--
作者：
Sellers,JR;Goodson,HV
通讯作者：
Goodson,HV
修饰蛋白质上的预选位点：肌球蛋白重链的残基 633-642 是肌动蛋白结合位点的一部分。
DOI：
10.1073/pnas.85.20.7471
发表时间：
1988
影响因子：
11.1
作者：
Chaussepied,P;Morales,MF
通讯作者：
Morales,MF