Nucleation of polar actin filament assembly by a positively charged surface.
Nucleation of polar actin filament assembly by a positively charged surface.
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DOI：
10.1083/jcb.80.2.499
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发表时间：
1979-02
期刊：
影响因子：
--
通讯作者：
Spudich JA
中科院分区：
文献类型：
--
作者：
Brown SS;Spudich JA
聚赖氨酸包被的聚苯乙烯珠可以使单体肌动蛋白的极性组装成核成丝状形式。这种成核作用已经通过生物化学和结构实验的结合得到了证实。聚赖氨酸包被的珠子加速肌动蛋白组装的速率，如通过两种不同的生物化学测定所检测到的。随后通过电子显微镜检查珠揭示了许多相似长度的肌动蛋白丝从珠辐射。ATP促进这种珠诱导的组装加速。用肌球蛋白片段S1装饰的肌丝表明，这些肌丝都具有相同的极性，箭头图案指向珠子。该系统的相关性在体外机制和它的有用性在其他研究进行了讨论。
Polylysine-coated polystyrene beads can nucleate polar assembly of monomeric actin into filamentous form. This nucleation has been demonstrated by a combination of biochemical and structural experiments. The polylysine-coated beads accelerate the rate of actin assembly as detected by two different biochemical assays. Subsequent examination of the beads by electron microscopy reveals numerous actin filaments of similar length radiating from the beads. ATP promotes this bead-induced acceleration of assembly. Decoration of the filaments with the myosin fragment S1 shows that these filaments all have the same polarity, with the arrowhead pattern pointing toward the bead. The relevance of the system to in vitro mechanisms and its usefulness in other studies are discussed.