Weber K, Schneider A, Westermann S, Müller N, Plessmann U
Max Planck Institute for Biophysical Chemistry, Department of Biochemistry, Göttingen, Germany.
FEBS Lett. 1997 Dec 8;419(1):87-91. doi: 10.1016/s0014-5793(97)01436-1.
Tubulin of Giardia lamblia, a representative of the oldest eukaryotes, was screened for posttranslational modifications. Mass spectrometry of the carboxy-terminal peptides documents a large number of variants. Both alpha- and beta-tubulin show polyglycylation with up to 20 and 15 extra glycyl residues respectively. Minor variants show a low level of glutamylation without or with glycylation. The glutamylation-specific antibody GT335 detects alpha- and beta-tubulin in immunoblots. The terminal tyrosine is fully retained in alpha-tubulin, which is completely acetylated at Lys-40. Thus except for the detyrosination/tyrosination cycle all posttranslational modifications known for higher eukaryotes are already present in Giardia.
对最古老的真核生物代表——蓝氏贾第鞭毛虫的微管蛋白进行了翻译后修饰筛选。对羧基末端肽段进行质谱分析记录了大量变体。α-微管蛋白和β-微管蛋白均显示多聚甘氨酰化，分别有多达20个和15个额外的甘氨酰残基。少数变体显示出低水平的谷氨酰化，有无甘氨酰化情况均有。谷氨酰化特异性抗体GT335在免疫印迹中可检测到α-微管蛋白和β-微管蛋白。α-微管蛋白中的末端酪氨酸完全保留，且在赖氨酸-40处完全乙酰化。因此，除了去酪氨酸化/酪氨酸化循环外，高等真核生物已知的所有翻译后修饰在蓝氏贾第鞭毛虫中均已存在。
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