Effect of histone deacetylase inhibitor trichostatin A (TSA) on the microtubular system of Tetrahymena.
Histone deacetylases can also influence acetylation of tubulin. In the present experiments, after 60 min of 10 microM trichostatin (TSA) treatment the structure and amount of tubulin and acetylated-tubulin were studied immunocytochemically, by using confocal microscopy and flow cytometry. In TSA-treated Tetrahymena cells deep fibres were never labeled with antibody to acetylated tubulin. Flow cytometry with anti acetylated-tubulin antibody demonstrated that in the contol cell populations there were weaker and stronger labelled parts. After TSA treatment in the weaker labeled part the cell number decreased, and in the stronger labeled part increased significantly: this means that after the histone deacetylase inhibitor TSA treatment the amount of acetylated-tubulin in numerous Tetrahymena cells is significantly elevated. Labeling with anti-tubulin antibody was not changed significantly. On the basis of these results we postulate that histone deacetylase also in Tetrahymena influences the acetylation of tubulin, and this enzyme is sensitive to TSA treatments.
Kovács
P
P
Department of Genetics, Cell- and Immunobiology, Semmelweis University, Budapest, Hungary. kovpet@dgci.sote.hu
Pállinger
Eva
E
Csaba
G
G
D000107:Acetylation / Q000187:drug effects; D000818:Animals; D005434:Flow Cytometry; D056572:Histone Deacetylase Inhibitors; D006877:Hydroxamic Acids / Q000494:pharmacology*; D007150:Immunohistochemistry; D018613:Microscopy, Confocal; D008870:Microtubules / Q000187:drug effects*; D013768:Tetrahymena / Q000187:drug effects*; D014404:Tubulin / Q000378:metabolism
D056572:Histone Deacetylase Inhibitors; D006877:Hydroxamic Acids; D014404:Tubulin; C012589:trichostatin A