Nucleic Acids Research, Vol 27, Issue 22 4427-4435, Copyright © 1999 by Oxford University Press
A Lusser, A Eberharter, A Loidl, M Goralik-Schramel, M Horngacher, H Haas and P Loidl
Purified histone acetyltransferase B (HAT-B) from maize consists of two
subunits, p50 and p45. Cloning of the cDNA and genomic DNA encoding the
catalytic subunit p50 revealed a consensus motif reminiscent of other
acetyltransferases. Internal peptide sequences and immunological studies
identified p45 as a protein related to the Retinoblastoma associated
protein Rbap. Antibodies against recombinant p50 were able to
immunoprecipitate the enzymatic activity of p50 as well as p45. Consistent
with the idea that HAT-B is involved in acetylation of newly synthesized
histone H4 during DNA replication, mRNA and protein levels are correlated
with S-phases during embryo germination. Inhibition of histone deacetylases
by HC toxin or Trichostatin A caused a decrease of the in vivo expression
of HAT-B mRNA. Regardless of its predominant cytoplasmic localization, a
significant proportion of HAT-B-p50 is present in nuclei, irrespective of
the cell cycle stage, suggesting an additional nuclear function.
ARTICLES
Analysis of the histone acetyltransferase B complex of maize embryos
Department of Microbiology, University of Innsbruck, Medical School, Fritz-Pregl-strasse 3, A-6020 Innsbruck, Austria.
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