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首页> 外文期刊>Journal of Molecular Biology >The location of ubiquitin in Lethocerus arthrin.
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The location of ubiquitin in Lethocerus arthrin.

机译：遍在蛋白在Lethocerus arthrin中的位置。

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Arthrin is a ubiquitinated actin that is present in flight muscles of some insects. In addition, it has been found in the malaria parasite Plasmodium falciparum. The role of this monoubiquitylation is not clear, and it does not appear to be associated with proteolytic degradation. The stoichiometry of arthrin to actin in Lethocerus indirect flight muscle, 1:6, suggests that there would be one arthrin molecule for each Tm-Tn (tropomyosin-troponin) complex. The appearance of arthrin after tropomyosin and troponin in Drosophila development is consistent with the Tm-Tn complex determining which actin subunit is targeted for conjugation with ubiquitin. We have used a new approach of three-dimensional reconstruction of helical filaments, the iterative helical real space reconstruction method, to extract segments of homogeneous arthrin out of long filaments where the conformation of the ubiquitin is more heterogeneous. Surprisingly, the location of the ubiquitin is on the face of actin subdomain 1, opposite to where tropomyosin binds in the "off" state, suggesting that there could not be a direct interaction between the ubiquitin and the tropomyosin. It is possible that the troponin complex in the "on" state that is bound to one actin strand makes an unfavorable contact with a ubiquitin molecule attached to the opposite actin strand. This might be the basis for a destabilization of the on state at rest length. Lys118 is the most likely residue to which the ubiquitin is conjugated, based upon fitting atomic structures of actin and ubiquitin into the reconstruction.
机译：Arthrin是泛素化的肌动蛋白，存在于某些昆虫的飞行肌肉中。另外，已经在疟疾寄生虫恶性疟原虫中发现了它。这种单泛素化的作用尚不清楚，并且似乎与蛋白水解降解无关。 Lethocerus间接飞行肌肉中arthrin与肌动蛋白的化学计量比为1：6，这表明每个Tm-Tn（原肌球蛋白-肌钙蛋白）复合物将有一个arthrin分子。果蝇发育中原肌球蛋白和肌钙蛋白后的arthrin出现与Tm-Tn复合体一致，后者确定哪个肌动蛋白亚基可与泛素结合。我们使用了螺旋丝的三维重建的新方法，即迭代螺旋实空间重构方法，从长丝中提取出均一的节油蛋白片段，而泛素的构象更加异质。出人意料的是，遍在蛋白的位置在肌动蛋白亚结构域1的表面，与原肌球蛋白在“关闭”状态下结合的位置相反，这表明遍在蛋白和原肌球蛋白之间可能没有直接的相互作用。与肌动蛋白链结合的处于“ on”状态的肌钙蛋白复合物可能与连接至相反肌动蛋白链的泛素分子发生不利接触。这可能是静止状态下导通状态不稳定的基础。基于肌动蛋白和泛素的原子结构适合重建，Lys118是最可能与泛素结合的残基。

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