Kuznitski L, Kuznitski Ia
Zh Evol Biokhim Fiziol. 1979 Sep-Oct;15(5):467-76.
In the paper we consider some aspects of evolution of actin, myosin, and Ca2+-binding proteins regulating their interaction. On the basis of the data recently obtained, we propose the following theses: 1. All types of motility in the living world where actin and myosin are involved, are based on active sliding of actin filaments along myosin filaments (or less organized myosin aggregates). 2. Ca2+-sensitivity of actin-myosin interaction is as old as actin and myosin themselves. Therefore, Ca2+-independent actomyosin ATPase found in vitro does not correspond to physiological sutuation and in this sense relfects an experimental artefact. 3. All proteins which regulate Ca2+-sensitivity of actin and myosin interaction, contain EF-hand structure. 4. It is generally believed that non-muscle cells, including Protozoa and Myxomycetes, contain all regulatory mechanisms which were described for muscles. However, in our opinion, troponin complex similar to that found in striated muscles, if present does not operate there.
在本文中，我们探讨了肌动蛋白、肌球蛋白以及调节它们相互作用的钙离子结合蛋白的进化的某些方面。基于最近获得的数据，我们提出以下论点：1. 生物界中所有涉及肌动蛋白和肌球蛋白的运动类型，都是基于肌动蛋白丝沿着肌球蛋白丝（或组织性较差的肌球蛋白聚集体）的主动滑动。2. 肌动蛋白 - 肌球蛋白相互作用的钙离子敏感性与肌动蛋白和肌球蛋白本身一样古老。因此，体外发现的不依赖钙离子的肌动球蛋白ATP酶并不符合生理情况，从这个意义上讲，它反映了一种实验假象。3. 所有调节肌动蛋白和肌球蛋白相互作用的钙离子敏感性的蛋白质都含有EF手结构。4. 人们普遍认为，包括原生动物和黏菌在内的非肌肉细胞含有所有已被描述的肌肉调节机制。然而，在我们看来，类似于在横纹肌中发现的肌钙蛋白复合物，即便存在于非肌肉细胞中也不起作用。
