| Literature DB >> 4020874 |
G Krämmer, M Singhofer-Wowra, K Seedorf, M Little, T Schedl.
Abstract
As the first step towards correlating structure and function of tubulin in the slime mold Physarum polycephalum we have elucidated the nucleotide sequence of a cDNA that appears to code for all but the last 25 to 30 C-terminal amino acids of a plasmodial alpha-tubulin. Differences in amino acid sequence from those of other alpha-tubulins are distributed fairly evenly throughout the sequence, although a relatively extensive conserved region is found in position 396 to 426 near the C terminus. A small region in position 298 to 307 contains a cluster of amino acid residues unique to Physarum alpha-tubulin. The sequence is 70% homologous to two yeast alpha-tubulins and about 83% homologous to five animal alpha-tubulins. A comparison of the homologies of all the known alpha-tubulins indicates that a large decrease in the accepted point mutation rate has occurred during the evolution of the metazoa, suggesting a major functional specialization of microtubules.Entities:
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Year: 1985 PMID: 4020874 DOI: 10.1016/0022-2836(85)90176-7
Source DB: PubMed Journal: J Mol Biol ISSN: 0022-2836 Impact factor: 5.469