Amino acid sequence data of α-tubulin from myxamoebae of Physarum polycephalum
| Autor: | Lesley Clayton, Monika Singhofer-Wowra, Melvyn Little, Keith Gull, Peter J. Dawson |
|---|---|
| Rok vydání: | 1986 |
| Předmět: |
Swine
Physarum polycephalum macromolecular substances medicine.disease_cause Physarum Tubulin Structural Biology medicine Animals Humans Amino Acid Sequence Molecular Biology Peptide sequence chemistry.chemical_classification Mutation biology Protein primary structure Mycetozoa biology.organism_classification Rats Amino acid chemistry Biochemistry Sea Urchins biology.protein Chickens |
| Zdroj: | Journal of Molecular Biology. 192:919-924 |
| ISSN: | 0022-2836 |
| Popis: | About 96% of the amino acid sequence of an alpha-tubulin from the slime mould Physarum polycephalum has been determined. Of 430 sequenced amino acids, 30 differ from the deduced amino acid sequence of a recently published alpha-tubulin complementary DNA from the plasmodial form of P. polycephalum. The myxamoebal alpha-tubulin differs from all other known alpha-tubulins in one of the last three C-terminal amino acids that are Gly-Glu-Tyr instead of the usual Glu-Glu-Tyr. These last three amino acids are preceded by 11 residues that appear to be particularly susceptible to mutation. No heterogeneity was found whilst sequencing the myxamoebal alpha-tubulin, indicating that only one type of alpha-tubulin is present in myxamoebae. This alpha-tubulin appears to be less conserved than the previously described plasmodial alpha-tubulin, supporting the hypothesis that the structural constraints on tubulin in axonemes have a significant effect on its rate of mutation. |
| Databáze: | OpenAIRE |
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