The dynamic character of core histone post-translational acetylation in the unicellular green alga Chlamydomonas reinhardtii was studied by tritiated acetate incorporation. Histone H3 is the major target of acetylation, steady state, and in pulse and pulse-chase analyses. Acetylation turnover rates were measured by tracer labeling under steady-state conditions. Half-lives of 1.5-3 min were found for penta- to mono-acetylation of H3, dynamically acetylated to the 30% level. Twenty percent of H3 was multi-acetylated, on average with 3. 2 acetyl-lysines, all with rapid turnover. Deacetylase inhibitor trichostatin A (TSA) caused doubling of average acetylation levels, primarily as penta-acetylated H3, but half of H3 was not acetylated at all. The level of histone H4 acetylation was only half that of H3 and a major fraction of mono- and di-acetylated forms appeared static. The dynamic fraction had an average half-life of 3.5 min with higher turnover rates for more highly acetylated H4 forms. TSA, inhibiting less effectively deacetylases active on H4, strongly increased multi-acetylated H4 levels and doubled average acetylation. As for H3, half of histone H4 remained unacetylated. Acetylation of histone H2B was low and of H2A was barely measurable. Despite turnover with half-lives of approximately 2 min, no increase beyond di-acetylation was seen upon TSA treatment.