Identification of an acetylation site of Chlamydomonas alpha-tubulin.
An acetylation site of Chlamydomonas axonemal alpha-tubulins was identified near, or within, the binding site of 6-11B-1, a monoclonal antibody specific for posttranslationally acetylated alpha-tubulins. In a first approach, axonemal proteins were hydrolyzed by formic acid, cyanogen bromide, or chymotrypsin and analyzed with immunoblots. The smallest alpha-tubulin peptide retained on nitrocellulose and containing antibody-binding site(s) was found to span amino acids 37-138 (alpha 37-138). A smaller antibody-binding peptide, identified as alpha 25-50, was obtained by complete digestion of alpha-tubulin with chymotrypsin. This fragment was purified by reversed-phase HPLC and assayed by its ability to bind 6-11B-1 in solution. Determination of the amino acid sequences of alpha 37-138 and alpha 25-50 showed that residue 40 in axonemal alpha-tubulin is epsilon N-acetyllysine. A sequence very similar to Chlamydomonas alpha 25-50 is found in the majority of alpha-tubulins analyzed so far. However, the corresponding region is markedly divergent in some alpha-tubulin isoforms from chicken, Drosophila, and yeast.[1]References
- Identification of an acetylation site of Chlamydomonas alpha-tubulin. LeDizet, M., Piperno, G. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
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