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Posttranslational modifications of α‐ and β‐tubulin in Giardia lamblia , an ancient eukaryote
Author(s) -
Weber Klaus,
Schneider André,
Westermann Stefan,
Müller Norbert,
Plessmann Uwe
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01436-1
Subject(s) - giardia lamblia , eukaryote , tubulin , giardia , protozoa , posttranslational modification , biology , microbiology and biotechnology , biochemistry , enzyme , genome , microtubule , gene
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 α‐ and β‐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 α‐ and β‐tubulin in immunoblots. The terminal tyrosine is fully retained in α‐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 .