Taurine Is Covalently Incorporated into Alpha-Tubulin.
Taurine Is Covalently Incorporated into Alpha-Tubulin.
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DOI:
10.1021/acs.jproteome.0c00147
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发表时间:
2020-08-07
影响因子:
4.4
通讯作者:
Sackett DL
中科院分区:
文献类型:
--
作者:
Olson MT;Yergey AL;Mukherjee K;Pergande MR;Bane SL;Cologna SM;Sackett DL
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 α-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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