Cloning and characterization of a myosin from characean alga, the fastest motor protein in the world

Cloning and characterization of a myosin from characean alga, the fastest motor protein in the world
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DOI:
10.1093/oxfordjournals.jbchem.a022699
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发表时间:
2000-06-01
影响因子:
2.7
通讯作者:
Yamamoto, K
Yamamoto, K
中科院分区:
生物学4区
文献类型:
--
作者:
Kashiyama, T;Kimura, N;Yamamoto, K

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相似文献

在特征性藻类中,一种非常规的肌凝蛋白在固定的肌动蛋白电缆上滑动运动,产生了非常快速的细胞质流动。这种滑动运动的速度是目前已知的许多分子马达中最快的。我们用特异性肌球蛋白抗体进行免疫筛选,克隆了一组编码该肌球蛋白重链的重叠cdna。该重链的分子量为248 kDa,具有保守的马达结构域、6个IQ基序、广泛的α -螺旋螺旋结构域和c端球状结构域。系统发育分析表明该肌球蛋白属于第XI类。
In characean algae, very rapid cytoplasmic streaming is generated by sliding movement of an unconventional myosin on fixed actin cables. The speed of this sliding movement is the fastest among many molecular motors known so far. We have cloned a set of overlapping cDNAs encoding the heavy chain of this myosin by immunoscreening with antibody raised against characean myosin. The molecular mass of this heavy chain is 248 kDa, and the protein has a conserved motor domain, six IQ motifs, an extensive alpha-helical coiled-coil domain, and a C-terminal globular domain. Phylogenetic analysis suggested that this myosin belongs to class XI.