Schneider A, Plessmann U, Felleisen R, Weber K
University of Fribourg, Institute of Zoology, Pérolles, Switzerland.
FEBS Lett. 1998 Jun 16;429(3):399-402. doi: 10.1016/s0014-5793(98)00644-9.
The alpha- and beta-tubulins present in cytoskeletons of Tritrichomonas mobilensis are extensively glutamylated. Automated sequencing and mass spectrometry of the carboxyterminal peptides identifies 4 glutamylation sites in alpha- and 2 sites in beta-tubulin. They are marked by asterisks in the terminal sequences GDEEEEDDG (alpha) and EGEEDEEAEA (beta). This is the first report that tubulin glutamylation can occur at multiple sites. Although T. mobilensis has four flagellae the tubulins lack polyglycylation. Thus glycylation is not necessary for formation or function of axonemal microtubules. Alpha-tubulin is completely acetylated at lysine 40 and shows no tyrosine cycle. Peptide sequences establish two distinct beta-tubulins.
活跃三毛滴虫细胞骨架中的α-微管蛋白和β-微管蛋白存在广泛的谷氨酰化修饰。对羧基末端肽段进行自动测序和质谱分析,确定α-微管蛋白有4个谷氨酰化位点,β-微管蛋白有2个谷氨酰化位点。在末端序列GDEEEEDDG(α)和EGEEDEEAEA(β)中,这些位点用星号标记。这是关于微管蛋白谷氨酰化可在多个位点发生的首次报道。尽管活跃三毛滴虫有四条鞭毛,但微管蛋白缺乏多聚糖基化修饰。因此,糖基化对于轴丝微管的形成或功能并非必需。α-微管蛋白在赖氨酸40处完全乙酰化,且无酪氨酸循环。肽段序列确定了两种不同的β-微管蛋白。