Journal article
A Highly Conserved 3-Methylhistidine Modification Is Absent in Yeast Actin
Archives of biochemistry and biophysics, Vol.370(1), pp.105-111
10/01/1999
DOI: 10.1006/abbi.1999.1370
PMID: 10496983
Abstract
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.
Details
- Title: Subtitle
- A Highly Conserved 3-Methylhistidine Modification Is Absent in Yeast Actin
- Creators
- Hamid R Kalhor - Department of Chemistry and Biochemistry and the Molecular Biology Institute, University of California, Los Angeles, California, 90095Agnieszka Niewmierzycka - Department of Chemistry and Biochemistry and the Molecular Biology Institute, University of California, Los Angeles, California, 90095Kym F Faull - Department of Psychiatry and Behavioral Sciences and the Neuropsychiatric Institute, University of California, Los Angeles, California, 90095Xiaoyi Yao - Department of Biochemistry, University of Iowa College of Medicine, Iowa City, Iowa, 52242Stephanie Grade - Department of Biochemistry, University of Iowa College of Medicine, Iowa City, Iowa, 52242Steven Clarke - Department of Chemistry and Biochemistry and the Molecular Biology Institute, University of California, Los Angeles, California, 90095Peter A Rubenstein - Department of Biochemistry, University of Iowa College of Medicine, Iowa City, Iowa, 52242
- Resource Type
- Journal article
- Publication Details
- Archives of biochemistry and biophysics, Vol.370(1), pp.105-111
- Publisher
- Elsevier Inc
- DOI
- 10.1006/abbi.1999.1370
- PMID
- 10496983
- ISSN
- 0003-9861
- eISSN
- 1096-0384
- Language
- English
- Date published
- 10/01/1999
- Academic Unit
- Stead Family Department of Pediatrics; Biochemistry and Molecular Biology; Internal Medicine
- Record Identifier
- 9984025394802771
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