A highly conserved 3-methylhistidine modification is absent in yeast actin
| Autor: | Xiaoyi Yao, Agnieszka Niewmierzycka, Peter A. Rubenstein, Steven Clarke, Stephanie K. Grade, Kym F. Faull, Hamid Reza Kalhor |
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| Rok vydání: | 1999 |
| Předmět: |
Saccharomyces cerevisiae
Molecular Sequence Data Biophysics Spectrometry Mass Secondary Ion macromolecular substances Biochemistry Evolution Molecular Residue (chemistry) Candida albicans Animals Amino Acid Sequence Protein Methyltransferases Muscle Skeletal Molecular Biology Histidine Actin Conserved Sequence Phylogeny biology Physarum Sequence Homology Amino Acid Methylation biology.organism_classification Methylhistidines Dictyostelium Yeast Actins Peptide Fragments Rabbits Sequence Alignment |
| Zdroj: | Archives of biochemistry and biophysics. 370(1) |
| ISSN: | 0003-9861 |
| Popis: | To identify a protein histidine methyltransferase from Saccharomyces cerevisiae, we examined purified actin for the presence of the highly conserved 3-methylhistidine residue at position 73 by amino acid analysis of the whole protein and by amino acid analysis and mass spectrometry of the corresponding tryptic fragment. Surprisingly, we found that His-73 is not modified. A similar lack of modification was also found in actin from the yeast Candida albicans, while rabbit muscle actin revealed the expected 3-methylhistidine residue. Phylogenetic analysis of actin sequences suggests that this modification was introduced in evolution after the divergence of yeast from higher eukaryotic organisms, including unicellular eukaryotes such as Acanthamoeba, Dictyostelium, and Physarum, whose actins contain 3-methylhistidine. Our methodology for the analytical determination of 3-methylhistidine in actin offers an improved approach for investigating histidine methylation in proteins. |
| Databáze: | OpenAIRE |
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