PMID: 558199May 1, 1977Paper

Modification of tubulin by tyrosylation in cells and extracts and its effect on assembly in vitro

The Journal of Cell Biology
D Raybin, M Flavin

Abstract

A post-translational modification of tubulin with potential regulatory significance has been revealed by the discovery of an enzyme (tubulin-tyrosine ligase) in brain extracts which can add a tyrosine residue to the alpha chain, apparently through peptide bond linkage to a C-terminal glutamate. We have investigated whether this modification also occurs in vivo, and whether it alters the extent to which tubulin can assemble in vitro. Cytoplasmic tubulin purified from bovine brain by cycles of assembly was shown to be partially tyrosylated. Carboxypeptidase A digestion of isolated alpha chains liberated about 0.3 equivalent of tyrosine. Brief digestion of native tubulin increased the proportion of alpha chains which could be tyrosylated by ligase, from 25 to 45%. The tubulin assembled to the same extent before and after carboxypeptidase treatment. When tubulin was purified after introducing labeled tyrosine with ligase, the labeled species assembled in the same proportion as unlabeled. Thus tubulin can be incorporated into microbubules in vitro with or without C-terminal tyrosine. An apparent resolution of alpha chain into two components by hydroxylapatite chromatography was shown not to be due to the presence or absence of C-ter...Continue Reading

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Citations

Jan 1, 1996·Cell Motility and the Cytoskeleton·C S Spittle, L Cassimeris
Jun 1, 1991·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·J C Bulinski, G G Gundersen
Jun 1, 1991·Neurochemical Research·J J Bray, R G Mills
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Nov 17, 2011·Nature Reviews. Molecular Cell Biology·Carsten Janke, Jeannette Chloë Bulinski
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May 26, 1999·Proceedings of the National Academy of Sciences of the United States of America·J P EiserichB A Freeman

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