在微管的表面晶格上：螺旋起始点、原纤维数量、接缝和旋向。
On the surface lattice of microtubules: helix starts, protofilament number, seam, and handedness.
作者信息
Mandelkow E M, Schultheiss R, Rapp R, Müller M, Mandelkow E
出版信息
J Cell Biol. 1986 Mar;102(3):1067-73. doi: 10.1083/jcb.102.3.1067.
Abstract
The tubulin monomers of brain microtubules reassembled in vitro are arranged on a 3-start helix, irrespective of whether the number of protofilaments is 13 or 14. The dimer packing is that of the B-lattice described for flagellar microtubules. This implies that the tubulin core of microtubules contains at least one helical discontinuity. Neither 5-start nor 8-start helices have a physical significance and thus cannot be implicated in models of microtubule elongation, but the structure is compatible with elongation of protofilaments by dimers or protofilamentous oligomers. The inner and outer surfaces of the microtubule wall can be visualized by propane jet freezing, freeze fracturing, and metal replication, at a resolution of at least 4 nm. The 3-start helix is left-handed, in contrast to a previous study based on negative staining and shadowing. The reasons for this discrepancy are discussed.
摘要
体外重新组装的脑微管的微管蛋白单体排列成三起始螺旋，无论原纤维数量是13还是14。二聚体堆积是鞭毛微管中描述的B晶格堆积。这意味着微管的微管蛋白核心至少包含一个螺旋间断。五起始螺旋和八起始螺旋都没有实际意义，因此不能与微管伸长模型相关，但该结构与二聚体或原纤维状寡聚体引起的原纤维伸长是相容的。微管壁的内表面和外表面可以通过丙烷喷射冷冻、冷冻断裂和金属复型来观察，分辨率至少为4纳米。与之前基于负染色和阴影的研究相反，三起始螺旋是左手螺旋。讨论了这种差异的原因。
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