果糖二磷酸醛缩酶与含肌动蛋白丝相互作用的电子显微镜研究。
An electron microscope study of the interaction between fructose diphosphate aldolase and actin-containing filaments.
作者信息
Morton D J, Clarke F M, Masters C J
出版信息
J Cell Biol. 1977 Sep;74(3):1016-23. doi: 10.1083/jcb.74.3.1016.
Abstract
The interaction of fructose diphosphate aldolase with F-actin, F-actin-tropomyosin, and F-actin-tropomyosin-troponin has been studied by using negative staining. In the absence of troponin, minor aggregates of aldolase and the F-actin filaments are formed. A well-ordered lattice structure is only formed in the case of the fully reconstituted filament when the filament-to-filament spacing is 18nm, and the cross-bridge spacing is 38.7 nm. Evidence is presented that the lattice is due to an interaction between troponin and aldolase. The minimum subunit structure of troponin, still capable of giving rise to a lattice, is the troponin-IT complex, which indicates that troponin-C is not involved in aldolase binding.
摘要
利用负染色法研究了果糖二磷酸醛缩酶与F-肌动蛋白、F-肌动蛋白-原肌球蛋白以及F-肌动蛋白-原肌球蛋白-肌钙蛋白之间的相互作用。在没有肌钙蛋白的情况下，会形成醛缩酶和F-肌动蛋白丝的微型聚集体。只有在完全重构的细丝且细丝间间距为18nm、横桥间距为38.7nm时，才会形成有序的晶格结构。有证据表明，该晶格是由于肌钙蛋白与醛缩酶间的相互作用形成的。仍能产生晶格的肌钙蛋白最小亚基结构是肌钙蛋白-I-T复合物，这表明肌钙蛋白-C不参与醛缩酶的结合。
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