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Taurine is Covalently Incorporated into Alpha Tubulin

preprint
submitted on 27.12.2019, 21:14 and posted on 31.12.2019, 20:54 by Matthew T Olson, Alfred L Yergey, Kamalika Mukherjee, melissa Pergande, susan Bane, Stephanie Cologna, Dan Sackett
We use various methods of high resolution mass spectrometry to demonstrate that taurine is covalently attached to the carboxyl terminus of alpha Tubulin from avian erythrocytes. The alpha Tubulin terminal residue, a tyrosine, must already be removed before covalent addition of taurine, via a known cycle of de-tyrosination and re-tyrosination. Taurination appears to stop this cycle. Taurine is the most abundant free amino acid in the body but this is the first time that it has been shown to be covalently incorporated into any protein.

Funding

Intramural research program of. NICHD, NIH

NIH-1R15GM093941

History

Email Address of Submitting Author

sackettd@mail.nih.gov

Institution

Eunice Kennedy Shriver National Institute of Child Health and Human Development, NIH

Country

United States

ORCID For Submitting Author

0000-0002-3492-1866

Declaration of Conflict of Interest

No conflict of interest

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in Journal of Proteome Research

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