Overexpression of the Aspergillus nidulans histone 4 acetyltransferase EsaA increases activation of secondary metabolite production

Summary Regulation of secondary metabolite (SM) gene clusters in Aspergillus nidulans has been shown to occur through cluster‐specific transcription factors or through global regulators of chromatin structure such as histone methyltransferases, histone deacetylases, or the putative methyltransferase...

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Bibliographic Details
Published in:Molecular microbiology 2012-10, Vol.86 (2), p.314-330
Main Authors: Soukup, Alexandra A., Chiang, Yi-Ming, Bok, Jin Woo, Reyes-Dominguez, Yazmid, Oakley, Berl R., Wang, Clay C. C., Strauss, Joseph, Keller, Nancy P.
Format: Article
Language:English
Subjects:
Acetylation
Amino Acid Motifs
Aspergillus nidulans - chemistry
Aspergillus nidulans - enzymology
Aspergillus nidulans - genetics
Aspergillus nidulans - metabolism
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Fungal Proteins - genetics
Fungal Proteins - metabolism
Fungi
Gene Expression
Gene Expression Regulation, Fungal
Histone Acetyltransferases - genetics
Histone Acetyltransferases - metabolism
Histones - chemistry
Histones - metabolism
Metabolites
Microbiology
Miscellaneous
Mutation
Mycology
Proteins
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Summary:Summary Regulation of secondary metabolite (SM) gene clusters in Aspergillus nidulans has been shown to occur through cluster‐specific transcription factors or through global regulators of chromatin structure such as histone methyltransferases, histone deacetylases, or the putative methyltransferase LaeA. A multicopy suppressor screen for genes capable of returning SM production to the SM deficient ΔlaeA mutant resulted in identification of the essential histone acetyltransferase EsaA, able to complement an esa1 deletion in Saccharomyces cereviseae. Here we report that EsaA plays a novel role in SM cluster activation through histone 4 lysine 12 (H4K12) acetylation in four examined SM gene clusters (sterigmatocystin, penicillin, terrequinone and orsellinic acid), in contrast to no increase in H4K12 acetylation of the housekeeping tubA promoter. This augmented SM cluster acetylation requires LaeA for full effect and correlates with both increased transcript levels and metabolite production relative to wild type. H4K12 levels may thus represent a unique indicator of relative production potential, notably of SMs.
ISSN:0950-382X
1365-2958
DOI:10.1111/j.1365-2958.2012.08195.x