Journal article
KdmA, a histone H3 demethylase with bipartite function, differentially regulates primary and secondary metabolism in Aspergillus nidulans
Agnieszka Gacek-Matthews, Luke M Noble, Clemens Gruber, Harald Berger, Michael Sulyok, Ana T Marcos, Joseph Strauss, Alex Andrianopoulos
Molecular Microbiology | WILEY | Published : 2015
DOI: 10.1111/mmi.12977
Abstract
Aspergillus nidulans kdmA encodes a member of the KDM4 family of jumonji histone demethylase proteins, highly similar to metazoan orthologues both within functional domains and in domain architecture. This family of proteins exhibits demethylase activity towards lysines 9 and 36 of histone H3 and plays a prominent role in gene expression and chromosome structure in many species. Mass spectrometry mapping of A. nidulans histones revealed that around 3% of bulk histone H3 carried trimethylated H3K9 (H3K9me3) but more than 90% of histones carried either H3K36me2 or H3K36me3. KdmA functions as H3K36me3 demethylase and has roles in transcriptional regulation. Genetic manipulation of KdmA levels i..
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Awarded by Austrian Science Fund FWF
Awarded by Vienna Science and Technology Fund
Awarded by Spanish Ministerio de Ciencia e Innovacion
Funding Acknowledgements
Work in Austria was funded by the Austrian Science Fund FWF grant number S10003-B17 and by the Vienna Science and Technology Fund Project LS 09-042. Work in Australia was funded by grants from the Australian Research Council and Howard Hughes Medical Institute to AA, and by the Spanish Ministerio de Ciencia e Innovacion (BFU2008-04306) for work performed by AM in the laboratory of David Canovas. Microarray slides and experimental protocols were provided by the Pathogen Functional Genomics Resource Center (PFGRC) through NIAID, deletion cassettes by the Fungal Genetics Stock Centre. We thank the Oakley and Aguirre laboratories for strains, and Q. Lang for photography. We are grateful to Joan Tilburn and David Canovas for helpful discussions on penicillin production, light regulation and for critically reading the manuscript.