• We are sorry, but NCBI web applications do not support your browser and may not function properly. More information
Logo of jcellbiolHomeThe Rockefeller University PressEditorsContactInstructions for AuthorsThis issue
J Cell Biol. Aug 1, 1986; 103(2): 571–579.
PMCID: PMC2113826

The acetylation of alpha-tubulin and its relationship to the assembly and disassembly of microtubules

Abstract

A tight association between Chlamydomonas alpha-tubulin acetyltransferase (TAT) and flagellar axonemes, and the cytoplasmic localization of both tubulin deacetylase (TDA) and an inhibitor of tubulin acetylation have been demonstrated by the use of calf brain tubulin as substrate for these enzymes. A major axonemal TAT of 130 kD has been solubilized by high salt treatment, purified, and characterized. Using the Chlamydomonas TAT with brain tubulin as substrate, we have studied the effects of acetylation on the assembly and disassembly of microtubules in vitro. We also determined the relative rates of acetylation of tubulin dimers and polymers. The acetylation does not significantly affect the temperature-dependent polymerization or depolymerization of tubulin in vitro. Furthermore, polymerization of tubulin is not a prerequisite for the acetylation, although the polymer is a better substrate for TAT than the dimer. The acetylation is sensitive to calcium ions which completely inhibit the acetylation of both dimers and polymers of tubulin. Acetylation of the dimer is not inhibited by colchicine; the effect of colchicine on acetylation of the polymer can be explained by its depolymerizing effect on the polymer.

Full Text

The Full Text of this article is available as a PDF (860K).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Allfrey VG, Di Paola EA, Sterner R. Protein side-chain acetylations. Methods Enzymol. 1984;107:224–240. [PubMed]
  • ALLFREY VG, FAULKNER R, MIRSKY AE. ACETYLATION AND METHYLATION OF HISTONES AND THEIR POSSIBLE ROLE IN THE REGULATION OF RNA SYNTHESIS. Proc Natl Acad Sci U S A. 1964 May;51:786–794. [PMC free article] [PubMed]
  • Brunke KJ, Collis PS, Weeks DP. Post-translational modification of tubulin dependent on organelle assembly. Nature. 1982 Jun 10;297(5866):516–518. [PubMed]
  • Gershey EL, Vidali G, Allfrey VG. Chemical studies of histone acetylation. The occurrence of epsilon-N-acetyllysine in the f2a1 histone. J Biol Chem. 1968 Oct 10;243(19):5018–5022. [PubMed]
  • Greer K, Maruta H, L'Hernault SW, Rosenbaum JL. Alpha-tubulin acetylase activity in isolated Chlamydomonas flagella. J Cell Biol. 1985 Dec;101(6):2081–2084. [PMC free article] [PubMed]
  • Lefebvre PA, Silflow CD, Wieben ED, Rosenbaum JL. Increased levels of mRNAs for tubulin and other flagellar proteins after amputation or shortening of Chlamydomonas flagella. Cell. 1980 Jun;20(2):469–477. [PubMed]
  • L'Hernault SW, Rosenbaum JL. Chlamydomonas alpha-tubulin is posttranslationally modified in the flagella during flagellar assembly. J Cell Biol. 1983 Jul;97(1):258–263. [PMC free article] [PubMed]
  • L'Hernault SW, Rosenbaum JL. Reversal of the posttranslational modification on Chlamydomonas flagellar alpha-tubulin occurs during flagellar resorption. J Cell Biol. 1985 Feb;100(2):457–462. [PMC free article] [PubMed]
  • L'Hernault SW, Rosenbaum JL. Chlamydomonas alpha-tubulin is posttranslationally modified by acetylation on the epsilon-amino group of a lysine. Biochemistry. 1985 Jan 15;24(2):473–478. [PubMed]
  • Murray JM. Disassembly and reconstitution of a membrane-microtubule complex. J Cell Biol. 1984 Apr;98(4):1481–1487. [PMC free article] [PubMed]
  • Piperno G, Fuller MT. Monoclonal antibodies specific for an acetylated form of alpha-tubulin recognize the antigen in cilia and flagella from a variety of organisms. J Cell Biol. 1985 Dec;101(6):2085–2094. [PMC free article] [PubMed]
  • Rosenbaum JL, Binder LI, Granett S, Dentler WL, Snell W, Sloboda R, Haimo L. Directionality and rate of assembly of chick brain tubulin onto pieces of neurotubules, flagellar axonemes, and basal bodies. Ann N Y Acad Sci. 1975 Jun 30;253:147–177. [PubMed]
  • Rosenbaum JL, Moulder JE, Ringo DL. Flagellar elongation and shortening in Chlamydomonas. The use of cycloheximide and colchicine to study the synthesis and assembly of flagellar proteins. J Cell Biol. 1969 May;41(2):600–619. [PMC free article] [PubMed]
  • Sloboda RD, Rosenbaum JL. Decoration and stabilization of intact, smooth-walled microtubules with microtubule-associated proteins. Biochemistry. 1979 Jan 9;18(1):48–55. [PubMed]
  • Swan JA, Solomon F. Reformation of the marginal band of avian erythrocytes in vitro using calf-brain tubulin: peripheral determinants of microtubule form. J Cell Biol. 1984 Dec;99(6):2108–2113. [PMC free article] [PubMed]
  • Travis GH, Colavito-Shepanski M, Grunstein M. Extensive purification and characterization of chromatin-bound histone acetyltransferase from Saccharomyces cerevisiae. J Biol Chem. 1984 Dec 10;259(23):14406–14412. [PubMed]
  • Witman GB, Carlson K, Berliner J, Rosenbaum JL. Chlamydomonas flagella. I. Isolation and electrophoretic analysis of microtubules, matrix, membranes, and mastigonemes. J Cell Biol. 1972 Sep;54(3):507–539. [PMC free article] [PubMed]
  • Witman GB, Plummer J, Sander G. Chlamydomonas flagellar mutants lacking radial spokes and central tubules. Structure, composition, and function of specific axonemal components. J Cell Biol. 1978 Mar;76(3):729–747. [PMC free article] [PubMed]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

Formats: