Weber K, Schneider A, Müller N, Plessmann U
Max-Planck-Institute for Biophysical Chemistry, Department of Biochemistry, Goettingen, Germany.
FEBS Lett. 1996 Sep 9;393(1):27-30. doi: 10.1016/0014-5793(96)00848-4.
We have searched for post-translational modifications in tubulin of the diplomonad Giardia lamblia, which is a representative of the earliest branches in eukaryotic evolution. The carboxyterminal peptide of alpha-tubulin was isolated and characterized by automated sequencing and mass spectrometry. Some 60% of the peptide is unmodified, while the remainder shows various degrees of polyglycylation. The number of glycyl residues in the lateral side chain ranges from 2 to 23. All peptide species encountered end with alanine-tyrosine, indicating the absence of a detyrosination/tyrosination cycle. We conclude that tubulin-specific polyglycylation could be as old as tubulin and axonemal structures.
我们在双滴虫贾第虫的微管蛋白中寻找翻译后修饰,贾第虫是真核生物进化中最早分支的代表。α-微管蛋白的羧基末端肽通过自动测序和质谱进行分离和表征。约60%的肽未被修饰,其余部分显示出不同程度的多聚甘氨酰化。侧链中甘氨酰残基的数量范围为2至23。所有遇到的肽种类均以丙氨酸-酪氨酸结尾,表明不存在去酪氨酸化/酪氨酸化循环。我们得出结论,微管蛋白特异性多聚甘氨酰化可能与微管蛋白和轴丝结构一样古老。