The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.
Identification of an acetylation site of Chlamydomonas alpha-tubulin.
Open accessAbstract
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.
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Cites
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Microtubules containing acetylated alpha-tubulin in mammalian cells in culture.
Piperno, G., LeDizet, M., & Chang, X. J. (1987) · The Journal of cell biology · doi:10.1083/jcb.104.2.289 · Cited by 873
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Self-citationGundersen, G. G., Kalnoski, M. H., & Bulinski, J. C. (1984) · Cell · doi:10.1016/0092-8674(84)90273-3 · Cited by 533
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Nucleotide and corresponding amino acid sequences encoded by α and β tubulin mRNAs
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Self-citationComplete amino acid sequence of alpha-tubulin from porcine brain.
Ponstingl, H., Krauhs, E., Little, M., & Kempf, T. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.5.2757 · Cited by 272
Expression of human alpha-tubulin genes: interspecies conservation of 3' untranslated regions.
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Cited by
Khalifa, A. A. Z., Ichikawa, M., Dai, D., Kubo, S., Black, C. S., Peri, K., McAlear, T. S., Veyron, S., Yang, S. K., Vargas, J., et al. (2020) · eLife · doi:10.7554/elife.52760 · Cited by 1,676
The tubulin code and its role in controlling microtubule properties and functions
Janke, C., & Magiera, M. M. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0214-3 · Cited by 956
MEC-17 is an α-tubulin acetyltransferase
Akella, J. S., Wloga, D., Kim, J., Starostina, N. G., Lyons-Abbott, S., Morrissette, N. S., Dougan, S. T., Kipreos, E. T., & Gaertig, J. (2010) · Nature · doi:10.1038/nature09324 · Cited by 489
Causes and Consequences of Microtubule Acetylation
Janke, C., & Montagnac, G. (2017) · Current Biology · doi:10.1016/j.cub.2017.10.044 · Cited by 312
Structure of the Decorated Ciliary Doublet Microtubule
Ma, M., Stoyanova, M., Rademacher, G., Dutcher, S. K., Brown, A., & Zhang, R. (2019) · Cell · doi:10.1016/j.cell.2019.09.030 · Cited by 290
Metadata
- Authors
- LeDizet, M., & Piperno, G.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1987-08
- Volume
- 84
- Issue
- 16
- Pages
- 5720-5724
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2072321275
- Cited by
- 320
- References
- 24
- FWCI
- 3.79
- Type
- journal article
- Language
- en
- Open access
- green
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