Taurine is Covalently Incorporated into Alpha Tubulin

31 December 2019, Version 1
This content is a preprint and has not undergone peer review at the time of posting.

Abstract

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.

Keywords

Taurine
tubulin
post translational modifications

Supplementary materials

Title
Description
Actions
Title
Taurine Tubulin 2019 12 26
Description
Actions

Comments

Comments are not moderated before they are posted, but they can be removed by the site moderators if they are found to be in contravention of our Commenting Policy [opens in a new tab] - please read this policy before you post. Comments should be used for scholarly discussion of the content in question. You can find more information about how to use the commenting feature here [opens in a new tab] .
This site is protected by reCAPTCHA and the Google Privacy Policy [opens in a new tab] and Terms of Service [opens in a new tab] apply.