Posttranslational modifications of α-tubulin of Toxoplasma gondii
Posttranslational modifications of α-tubulin of Toxoplasma gondii
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DOI：
10.1007/s00436-004-1220-7
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发表时间：
2004-11-01
影响因子：
2
通讯作者：
Lechtreck, KF
中科院分区：
文献类型：
--
作者：
Plessmann, U;Reiter-Owona, I;Lechtreck, KF
通过抗体和羧基端肽的生化分析，对弓形虫α-微管蛋白的翻译后修饰进行了表征。α-微管蛋白被乙酰化和谷氨酰化。最多有三个谷氨酸残基的侧链连接到T的Glu 445。弓形虫α-微管蛋白这些数据表明，α-微管蛋白上的谷氨酰化位点在广泛的物种中是保守的。
The posttranslational modifications of alpha-tubulin of Toxoplasma gondii were characterized by antibodies and biochemical analysis of the carboxy-terminal peptide. alpha-Tubulin is acetylated and glutamylated. Side chains with up to three glutamate residues are linked to Glu445 of T. gondii alpha-tubulin. The data suggest that the site of glutamylation on alpha-tubulin is conserved over a broad range of species.