ArticleThe EMBO journal1988
A survey of the alpha-tubulin gene family in chicken: unexpected sequence heterogeneity in the polypeptides encoded by five expressed genes.
Article in The EMBO journal, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 47 citations in OpenAlex.
- Tubulin isotypes optimize distinct spindle positioning mechanisms during yeast mitosis.The Journal of cell biology · 2021Article
- Interaction of Recombinant Gallus gallus SEPT5 and Brain Proteins of H5N1-Avian Influenza Virus-Infected Chickens.Proteomes · 2017Article
- Are tubulin isotypes functionally significant.Molecular biology of the cell · 1993Review
- Dynamics of microtubules from erythrocyte marginal bands.Molecular biology of the cell · 1993Article
- Heritable retroviral transgenes are highly expressed in chickens.Proceedings of the National Academy of Sciences of the United States of America · 1991Article
- Evidence that introns arose at proto-splice sites.The EMBO journal · 1989Article
- The 5' splice site: phylogenetic evolution and variable geometry of association with U1RNA.Nucleic acids research · 1989Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
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Abstract
To characterize the alpha-tubulin gene family in chicken, we have isolated five chicken alpha-tubulin genes and determined the majority of the sequences of the encoded polypeptides. Three of these (c alpha 3, c alpha 5/6 and c alpha 8) encode novel, expressed alpha-tubulins that have not previously been analyzed, whereas one gene segment is a pseudogene and another appears capable of encoding a functional subunit (although we were unable to document its expression in a survey of chicken tissues). Together with two additional expressed, functional alpha-tubulins reported earlier, we conclude that the chicken alpha-tubulin family is comprised of at least five functional genes whose polypeptide products are substantially more heterogeneous than found in preceding analyses of vertebrate alpha-tubulins. Comparison of the amino acid sequences reveals that the five polypeptides are between 96 and 83% identical, with the extreme carboxy-terminal residues representing a highly heterogeneous variable domain. Since some alpha-tubulins undergo cyclic post-translational removal and readdition of a carboxy-terminal tyrosine, the notable sequence divergence in this domain suggests that individual tubulins probably participate to different extents in this modification cycle.
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