POSTTRANSLATIONAL GLUTAMYLATION OF ALPHA-TUBULIN
POSTTRANSLATIONAL GLUTAMYLATION OF ALPHA-TUBULIN
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DOI：
10.1126/science.1967194
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发表时间：
1990-01-05
期刊：
影响因子：
56.9
通讯作者：
DENOULET, P
中科院分区：
文献类型：
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作者：
EDDE, B;ROSSIER, J;DENOULET, P
神经元中微管蛋白的高度异质性主要在翻译后水平上受到控制。将细胞与[ 3 H]乙酸盐或[ 3 H]谷氨酸盐一起温育后，可以对α-微管蛋白的几种变体进行翻译后标记。通过高效液相色谱法纯化携带放射性部分的肽。这些肽的氨基酸分析、Edman降解测序和质谱分析导致了翻译后修饰的表征，该翻译后修饰由谷氨酸残基(Glu445)的γ-羧基的谷氨酰单元的连续添加组成。这种修饰位于α-微管蛋白的一个区域内，该区域对于微管蛋白与微管相关蛋白和钙的相互作用很重要，可以在调节微管动力学中发挥作用。
The high degree of tubulin heterogeneity in neurons is controlled mainly at the posttranslational level. Several variants of .alpha.-tubulin can be posttranslationally labeled after incubation of cells with [3H]acetate or [3H]glutamate. Peptides carrying the radioactive moiety were purified by high-performance liquid chromatography. Amino acid analysis, Edman degradation sequencing, and mass spectrometric analysis of these peptides led to the characterization of a posttranslational modification consisting of the successive addition of glutamyl units of the .gamma.-carboxyl group of a glutamate residue (Glu445). This modification, localized within a region of .alpha.-tubulin that is important in the interactions of tubulin with microtubule-associated proteins and calcium, could play a role in regulating microtubule dynamics.