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肌动蛋白的聚合极性

Polymerization polarity of actin.

作者信息

Hayashi T, Ip W

出版信息

J Mechanochem Cell Motil. 1976 Mar;3(3):163-9.

PMID:932564
Abstract

The actin polymer, like the thin filaments of muscle, is known to be polarized as demonstrated by the well known "HMM decoration" technique to give a "herringbone" pattern pointing in one direction. The question "Does polymer formation proceed unidirectionally, or bidirectionally?" was raised and tested experimentally. Short fragments of actin polymers were prepared, fully decorated with HMM and these decorated fragments were used as initiation centers for further actin polymerization without HMM. The resultant polymers showing both decorated and undecorated portions were examined and found to consist of a large majority of "spears" i.e., the added undecorated polymer extended in the direction opposite to that direction pointed by the "herringbone" pattern. However, a few cases of polymers indicating the opposite direction of polymerization were also found. Analysis leads to the conclusion that actin polymerization is unidirectional, although further experimentation is necessary to establish this completely.

摘要

肌动蛋白聚合物,就像肌肉中的细肌丝一样,已知是极化的,这一点通过著名的“HMM 标记”技术得到了证明,该技术会产生指向一个方向的“人字形”图案。于是有人提出并通过实验检验了“聚合物形成是单向进行还是双向进行?”这个问题。制备了肌动蛋白聚合物的短片段,用 HMM 完全标记,然后将这些标记的片段用作进一步肌动蛋白聚合(不使用 HMM)的起始中心。对所得的同时显示有标记和未标记部分的聚合物进行检查,发现其中绝大多数是“矛状”结构,即添加的未标记聚合物朝着与“人字形”图案所指方向相反的方向延伸。然而,也发现了少数聚合物显示出相反聚合方向的情况。分析得出结论,肌动蛋白聚合是单向的,不过要完全证实这一点还需要进一步实验。

相似文献

1
Polymerization polarity of actin.肌动蛋白的聚合极性
J Mechanochem Cell Motil. 1976 Mar;3(3):163-9.
2
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Cooperative rigor binding of myosin to actin is a function of F-actin structure.肌球蛋白与肌动蛋白的协同严格结合是F-肌动蛋白结构的一种功能。
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Polymerization of actin. VI. The polarity of the actin filaments in the acrosomal process and how it might be determined.肌动蛋白的聚合反应。VI. 顶体突起中肌动蛋白丝的极性及其确定方式。
J Cell Biol. 1979 Jun;81(3):608-23. doi: 10.1083/jcb.81.3.608.

引用本文的文献

1
In situ reconstitution of myosin filaments within the myosin-extracted myofibril in cultured skeletal muscle cells.在培养的骨骼肌细胞中,肌球蛋白提取的肌原纤维内肌球蛋白丝的原位重组。
J Cell Biol. 1982 Feb;92(2):324-32. doi: 10.1083/jcb.92.2.324.
2
Actin filaments elongate from their membrane-associated ends.肌动蛋白丝从其与膜相关的末端延伸。
J Cell Biol. 1981 Aug;90(2):485-94. doi: 10.1083/jcb.90.2.485.
3
Direct measurement of actin polymerization rate constants by electron microscopy of actin filaments nucleated by isolated microvillus cores.
通过对由分离的微绒毛核心成核的肌动蛋白丝进行电子显微镜观察,直接测量肌动蛋白聚合速率常数。
J Cell Biol. 1981 Mar;88(3):654-9. doi: 10.1083/jcb.88.3.654.
4
Mechanism of action of cytochalasin: evidence that it binds to actin filament ends.细胞松弛素的作用机制:它与肌动蛋白丝末端结合的证据。
J Cell Biol. 1981 Mar;88(3):487-91. doi: 10.1083/jcb.88.3.487.
5
Actin-binding protein promotes the bipolar and perpendicular branching of actin filaments.肌动蛋白结合蛋白促进肌动蛋白丝的双极和垂直分支。
J Cell Biol. 1980 Dec;87(3 Pt 1):841-8. doi: 10.1083/jcb.87.3.841.
6
Implications of treadmilling for the stability and polarity of actin and tubulin polymers in vivo.踏车行为对体内肌动蛋白和微管蛋白聚合物稳定性及极性的影响。
J Cell Biol. 1980 Jul;86(1):330-4. doi: 10.1083/jcb.86.1.330.
7
Nucleated polymerization of actin from the membrane-associated ends of microvillar filaments in the intestinal brush border.肌动蛋白从肠道刷状缘微绒毛丝的膜相关末端进行有核聚合。
J Cell Biol. 1982 Oct;95(1):223-33. doi: 10.1083/jcb.95.1.223.
8
Elongation of the fertilization tubule in Chlamydomonas: new observations on the core microfilaments and the effect of transient intracellular signals on their structural integrity.衣藻受精管的延长:关于核心微丝的新观察以及瞬时细胞内信号对其结构完整性的影响
J Cell Biol. 1983 Aug;97(2):522-32. doi: 10.1083/jcb.97.2.522.
9
Direct electron microscopic visualization of barbed end capping and filament cutting by intestinal microvillar 95-kdalton protein (villin): a new actin assembly assay using the Limulus acrosomal process.通过肠微绒毛95千道尔顿蛋白(绒毛蛋白)对带刺末端封端和细丝切割进行直接电子显微镜观察:一种使用鲎顶体过程的新肌动蛋白组装检测方法。
J Cell Biol. 1983 Apr;96(4):1097-107. doi: 10.1083/jcb.96.4.1097.
10
Polymerization of ADP-actin.二磷酸腺苷 - 肌动蛋白的聚合作用。
J Cell Biol. 1984 Sep;99(3):769-77. doi: 10.1083/jcb.99.3.769.