Nucleic Acids Research, 2003, Vol. 31, No. 14 3971-3981
© 2003 Oxford University Press
Histone deacetylases in fungi: novel members, new facts
Department of Molecular Biology, University of Innsbruck, Peter-Mayr-Strasse 4b, Innsbruck, A-6020, Austria
*To whom correspondence should be addressed. Tel: +43 512 507 3608; Fax: +43 512 507 2866; Email: stefan.graessle{at}uibk.ac.at
The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors
+AF306859, AF307341, AF537125 and AF537126
Acetylation is the most prominent modification on core histones that strongly affects nuclear processes such as DNA replication, DNA repair and transcription. Enzymes responsible for the dynamic equilibrium of histone acetylation are histone acetyltransferases (HATs) and histone deacetylases (HDACs). In this paper we describe the identification of novel HDACs from the filamentous fungi Aspergillus nidulans and the maize pathogen Cochliobolus carbonum. Two of the enzymes are homologs of Saccharomyces cerevisiae HOS3, an enzyme that has not been identified outside of the established yeast systems until now. One of these homologs, HosB, showed intrinsic HDAC activity and remarkable resistance against HDAC inhibitors like trichostatin A (TSA) when recombinant expressed in an Escherichia coli host system. Phylo genetic analysis revealed that HosB, together with other fungal HOS3 orthologs, is a member of a separate group within the classical HDACs. Immunological investigations with partially purified HDAC activities of Aspergillus showed that all classical enzymes are part of high molecular weight complexes and that a TSA sensitive class 2 HDAC constitutes the major part of total HDAC activity of the fungus. However, further biochemical analysis also revealed an NAD+-dependent activity that could be separated from the other activities by different types of chromatography and obviously represents an enzyme of the sirtuin class.
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