Posttranslational modifications of α- and β-tubulin in Giardia lamblia, an ancient eukaryote

被引:51
作者
Weber, K
Schneider, A
Westermann, S
Müller, N
Plessmann, U
机构
[1] Max Planck Inst Biophys Chem, Dept Biochem, D-37077 Gottingen, Germany
[2] Univ Fribourg, Inst Zool, CH-1700 Fribourg, Switzerland
[3] Univ Bern, Inst Parasitol, CH-3001 Bern, Switzerland
关键词
polyglutamylation; polyglycylation; posttranslational modification; tubulin; tyrosination; Giardia lamblia;
D O I
10.1016/S0014-5793(97)01436-1
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 detyrosinationl/tyrosination cycle all posttranslational modifications known for higher eukaryotes are already present in Giardia. (C) 1997 Federation of European Biochemical Societies.
引用
收藏
页码:87 / 91
页数:5
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