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微管蛋白氨甲酰化。微管组装中的功能性氨基基团。

Tubulin carbamoylation. Functional amino groups in microtubule assembly.

作者信息

Mellado W, Slebe J C, Maccioni R B

出版信息

Biochem J. 1982 Jun 1;203(3):675-81. doi: 10.1042/bj2030675.

Abstract

The characteristics of the carbamoylation of pig brain tubulin were examined by using the modification conditions with cyanate described previously [Mellado, Slebe + Maccioni (1980) Biochem. Int. I, 584--590]. The carbamoylation reaction resulted in an inhibition of microtubule assembly, which was dependent on the concentration of the modifying agent. This tubulin modification appears to inhibit the growth of microtubules. The presence of GTP did not protect tubulin against this inhibition. Electron microscopy showed a marked decrease in the number of tubules after carbamoylation, but no alterations were observed in the microtubule morphology. The incorporation of KN14CO into alpha- and beta-subunits with similar kinetics was also shown, and the carbamoylated residues were identified as epsilon-N-carbamoyl-lysine residues.

摘要

利用先前所述的氰酸盐修饰条件 [梅拉多、斯莱贝和马乔尼(1980年),《生物化学国际》第1卷,584 - 590页],对猪脑微管蛋白的氨甲酰化特性进行了研究。氨甲酰化反应导致微管组装受到抑制,这种抑制作用取决于修饰剂的浓度。这种微管蛋白修饰似乎会抑制微管的生长。鸟苷三磷酸(GTP)的存在并不能保护微管蛋白免受这种抑制。电子显微镜显示,氨甲酰化后微管数量显著减少,但微管形态未观察到改变。还表明,¹⁴C标记的氰酸盐以相似的动力学掺入α和β亚基,且氨甲酰化的残基被鉴定为ε-N-氨甲酰赖氨酸残基。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/99a0/1158283/64563f61d5e2/biochemj00376-0153-a.jpg

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