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Cited by 497

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Chlamydomonas .alpha.-tubulin is posttranslationally modified by acetylation on the .epsilon.-amino group of a lysine

L'Hernault, Steven W., Rosenbaum, Joel L.·1985·Biochemistry
DOI 10.1021/bi00323a034
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Abstract

Previous work has shown that the principal alpha-tubulin within Chlamydomonas reinhardtii flagellar axonemes differs from the major alpha-tubulin in the cell body. These two variants of alpha-tubulin are related to one another since posttranslational modification of the cell body form converts it to the axonemal form. When flagella are induced to assemble in the absence of de novo protein synthesis, tritiated acetate can be used to posttranslationally label alpha-tubulin in vivo, and under these conditions, no other flagellar polypeptides exhibit detectable labeling [L'Hernault, S. W., & Rosenbaum, J. L. (1983) J. Cell Biol. 97, 258-263]. In the present report, this labeling method has been used to provide material for chemical analysis of the tritiated moiety that is posttranslationally added to flagellar alpha-tubulin. This radioactivity was volatile after acid hydrolysis, suggesting that the posttranslational modification is the addition of neither an amino acid nor carbohydrate. Treatment of posttranslationally 3H-labeled alpha-tubulin with hydrazine yields radioactive acetylhydrazine, indicating that the moiety involved in posttranslational modification is an acetyl group. Analysis of complete proteolytic digests by thin-layer chromatography has revealed that this acetyl group is located on the epsilon-amino group of a flagellar alpha-tubulin lysine residue.

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Authors
L'Hernault, S. W., & Rosenbaum, J. L.
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
1985-01-15
Volume
24
Issue
2
Pages
473-478
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
DOI
10.1021/bi00323a034
OpenAlex
W2062584366
Cited by
497
References
0
FWCI
13.34
Type
journal article
Language
en
Open access
closed

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