期刊
JOURNAL OF PROTEOME RESEARCH
卷 19, 期 8, 页码 3184-3190出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jproteome.0c00147
关键词
post-translational modification; proteomics; mass spectrometry; sulfur; isotope cluster
资金
- Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institute of Health, DHHS
- University of Illinois at Chicago, Department of Chemistry, College of Liberal Arts and Sciences
- UIC DFI Fellowship
- State University of New York Binghamton
- NIH [1R15GM093941]
- EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT [ZIAHD008765] Funding Source: NIH RePORTER
Taurine is the most abundant free amino acid in the human body. It is found in relatively high concentrations (1-10 mM) in many animal tissues but not in plants. It has been studied since the early 1800s but has not been found to be covalently incorporated into proteins in any animal tissue. Taurine has been found in only one macromolecular complex as a post-transcriptional modification to mitochondrial tRNA. Tubulin is the subunit of microtubules found in all eukaryotic species and almost all eukaryotic cells and subject to numerous post-translational modifications (PTMs). An important PTM on alpha-tubulin is the removal and re-ligation of the final carboxyl residue, tyrosine. We here demonstrate that taurine can be covalently incorporated at the C-terminal end of alpha-tubulin in avian erythrocytes in a reaction that requires the de-tyrosination PTM and prevents the re-tyrosination PTM. Further, this is, to our knowledge, the first instance of taurine incorporation into a large protein.
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