Carp expresses fast skeletal myosin isoforms with altered motor functions and structural stabilities to compensate for changes in environmental temperature
Carp expresses fast skeletal myosin isoforms with altered motor functions and structural stabilities to compensate for changes in environmental temperature
复制标题
Carp 表达快速骨骼肌球蛋白亚型，具有改变的运动功能和结构稳定性，以补偿环境温度的变化
DOI：
10.1016/s0306-4565(97)00057-0
复制
发表时间：
1997
影响因子：
2.7
通讯作者：
T. Ooi
中科院分区：
文献类型：
--
作者：
S. Watabe;Y. Hirayama;M. Nakaya;M. Kakinuma;K. Kikuchi;Xiao;S. Kanoh;S. Chaen;T. Ooi
1. 与适应 30°C 的鲤鱼相比，适应 10°C 的鲤鱼的肌球蛋白及其亚片段-1 (Sl) 显示出更高的肌动蛋白激活的 Mg 2+-ATP 酶活性和更低的热稳定性。因此，在 3 至 23°C 的任何测量温度下，10°C 适应的鲤鱼肌球蛋白的丝速度都高于 30°C 的丝速度。 C-驯化的鲤鱼肌球蛋白。 2. 2. 从热驯化的鲤鱼中分离出三种编码肌球蛋白重链的 cDNA 克隆。 10°C和30°C类型分别在适应10°C和30°C的鲤鱼中占主导地位，而中间型在适应10°C的鲤鱼中占次要成分，其DNA核苷酸和推导的氨基酸序列均介于10°C和30°C类型之间。 3. 3. 三种类型的肌球蛋白杆均表现出典型的α-螺旋卷曲螺旋结构。 DSC扫描表明，由适应10℃的鲤鱼制备的肌球蛋白棒的热稳定性低于由适应30℃的鲤鱼制备的肌球蛋白棒，这表明冷适应鲤鱼肌球蛋白的低热稳定性普遍存在于整个分子中。 4. 4.从热驯化的鲤鱼中分离出编码肌球蛋白碱轻链的cDNA克隆。 Northern印迹分析表明，30°C驯化的鲤鱼中LC3 LC1 mRNA的比率（3.92）显着高于10°C驯化的鲤鱼（3.10）。
1. Myosin and its subfragment-1 (Sl) from carp acclimated to 10° C showed higher actin-activated Mg 2+-ATPase activity and lower thermostability than their counterparts from carp acclimated to 30° C. Accordingly, filament velocity for the 10° C-acclimated carp myosin was higher at any measuring temperatures from 3 to 23° C than that for the 30° C-acclimated carp myosin. 2. 2. Three types of cDNA clones encoding myosin heavy chains were isolated from thermally acclimated carp. The 10 and 30° C types were predominating in carp acclimated to 10 and 30° C, respectively, whereas the intermediate type was found as a minor component in the 10° C-acclimated carp with an intermediate feature in both DNA nucleotide and deduced amino acid sequences between those of the 10 and 30° C types. 3. 3. The three types of myosin rod all showed a typical coiled-coil structure of α-helices. DSC scans demonstrated that myosin rod prepared from carp acclimated to 10° C had a lower thermostability than that from carp acclimated to 30° C, showing that low thermostability in cold-acclimated carp myosin prevails over the entire molecule. 4. 4. cDNA clones encoding myosin alkali light chains were isolated from thermally acclimated carp. Northern blot analysis showed that the ratios of LC3 LC1 mRNAs were significantly higher (3.92) in the 30° C-than 10° C-acclimated (3.10) carp.
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
肌球蛋白的分子遗传学。
影响因子：
16.6
作者：
EmersonJr,CP;Bernstein,SI
通讯作者：
Bernstein,SI