Histone acetylation: plants and fungi as model systems for the investigation of histone deacetylases

Graessle, Stefan; Loidl, Peter; Brosch, Gerald

doi:10.1007/pl00000894

Cited by 38 publications

(32 citation statements)

References 155 publications

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“…Like other organisms, filamentous fungi have multiple HDACs (7,11,22,23,40). Potential mechanisms of toxin resistance that could be detected by fractionation of the HDACs of C. carbonum could be a novel HDAC activity, reduced levels of sensitive HDAC activity, higher levels of resistant HDAC activity, or conversion of a normally sensitive HDAC to resistance by posttranslational modification.…”

Section: Resultsmentioning

confidence: 99%

“…As a further investigation into the possibility that resistance is the result of qualitative differences among the HDACs of toxin-resistant and toxin-sensitive isolates, we examined the structure and expression of the C. carbonum HDAC genes. N. crassa, A. nidulans, and C. carbonum have HDACs related to yeast RPD3, HDA1, HOS2, and HOS3, but apparently do not have a homolog of yeast HOS1 (7,22,23). This is based on several attempts to find such a gene by using PCR primers based on HOS1, and on BLAST searching with all of the known fungal HDAC genes against the completed genomes of N. crassa (http://www-genome.wi.mit.edu), A. nidulans (http://microbial-.cereon.com), C. heterostrophus (http://www.nadii.com), and the basidiomycete Phanerochaete chrysosporium (http://www.jgi.doe.gov/programs/whiterot.htm).…”

Section: Resultsmentioning

confidence: 99%

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Characterization of Inhibitor-Resistant Histone Deacetylase Activity in Plant-Pathogenic Fungi

et al. 2002

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HC-toxin, a cyclic peptide made by the filamentous fungus Cochliobolus carbonum, is an inhibitor of histone deacetylase (HDAC) from many organisms. It was shown earlier that the HDAC activity in crude extracts of C. carbonum is relatively insensitive to HC-toxin as well as to the chemically unrelated HDAC inhibitors trichostatin and D85, whereas the HDAC activity of Aspergillus nidulans is sensitive (G. Brosch et al., Biochemistry 40:12855-12863, 2001). Here we report that HC-toxin-resistant HDAC activity was present in other, but not all, plant-pathogenic Cochliobolus species but not in any of the saprophytic species tested. The HDAC activities of the fungi Alternaria brassicicola and Diheterospora chlamydosporia, which also make HDAC inhibitors, were resistant. The HDAC activities of all C. carbonum isolates tested, except one non-toxin-producing isolate, were resistant. In a cross between a sensitive isolate and a resistant isolate, resistance genetically cosegregated with HC-toxin production. When fractionated by anion-exchange chromatography, extracts of resistant and sensitive isolates and species had two peaks of HDAC activity, one that was fully HC-toxin resistant and a second that was larger and sensitive. The first peak was consistently smaller in extracts of sensitive fungi than in resistant fungi, but the difference appeared to be insufficiently large to explain the differential sensitivities of the crude extracts. Differences in mRNA expression levels of the four known HDAC genes of C. carbonum did not account for the observed differences in HDAC activity profiles. When mixed together, resistant extracts protected extracts of sensitive C. carbonum but did not protect other sensitive Cochlibolus species or Neurospora crassa. Production of this extrinsic protection factor was dependent on TOXE, the transcription factor that regulates the HC-toxin biosynthetic genes. The results suggest that C. carbonum has multiple mechanisms of self-protection against HC-toxin.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Characterization of Inhibitor-Resistant Histone Deacetylase Activity in Plant-Pathogenic Fungi

et al. 2002

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“…The situation has become even more complex because proteins with high sequence similarities to HDACs are also present in archaea and bacteria, strongly suggesting that in eukaryotes the targets of HDACs are not confined to core histones. As a model organism for lower eukaryotes, the filamentous fungus A. nidulans has only four classical HDAC genes: one gene for each of the class 1 enzymes RpdA and HosA (19) and one gene each for HdaA and HosB, both of which are class 2 HDACs (20). However, in A. nidulans enzymatic activity was demonstrated only for RpdA and HdaA, both of which act in large enzymatic protein complexes (56).…”

Section: Discussionmentioning

confidence: 99%

HdaA, a Major Class 2 Histone Deacetylase of Aspergillus nidulans , Affects Growth under Conditions of Oxidative Stress

et al. 2005

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Histone deacetylases (HDACs) catalyze the removal of acetyl groups from the -amino group of distinct lysine residues in the amino-terminal tail of core histones. Since the acetylation status of core histones plays a crucial role in fundamental processes in eukaryotic organisms, such as replication and regulation of transcription, recent research has focused on the enzymes responsible for the acetylation/deacetylation of core histones. Very recently, we showed that HdaA, a member of the Saccharomyces cerevisiae HDA1-type histone deacetylases, is a substantial contributor to total HDAC activity in the filamentous fungus Aspergillus nidulans. Now we demonstrate that deletion of the hdaA gene indeed results in the loss of the main activity peak and in a dramatic reduction of total HDAC activity. In contrast to its orthologs in yeast and higher eukaryotes, HdaA has strong intrinsic activity as a protein monomer when expressed as a recombinant protein in a prokaryotic expression system. In vivo, HdaA is involved in the regulation of enzymes which are of vital importance for the cellular antioxidant response in A. nidulans. Consequently, ⌬hdaA strains exhibit significantly reduced growth on substrates whose catabolism generates molecules responsible for oxidative stress conditions in the fungus. Our analysis revealed that reduced expression of the fungal catalase CatB is jointly responsible for the significant growth reduction of the hdaA mutant strains.In eukaryotic organisms, DNA and highly basic nuclear proteins, the histones, constitute the nucleosome, which is the essential structural subunit of the chromatin. The fact that the N-terminal extensions of the core histones contain distinct sites for various posttranslational modifications alters our view of chromatin as being a static entity for the efficient packing of the genomic DNA into the nucleus of the cell. Today it is accepted that, in addition to its structural role, chromatin has an important regulatory function during DNA replication and repair, cell cycle control, cell aging, and transcription (for a review, see reference 59).Antagonistic enzymes such as kinases/phosphatases (10, 39), histone methyltransferases/demethylases (for a review, see reference 9), and histone acetyltransferases/deacetylases (for a review, see reference 38) are responsible for a dynamic equilibrium of chromatin regulating modifications of the histone tails.The acetylation of distinct lysine residues of H2A, H2B, H3, and H4 is the most prominent dynamic histone modification allowing or denying the access of numerous regulatory proteins, such as transcription factors, to distinct regions of genomic DNA. Although histone acetylation is by far the beststudied type of histone modification, our understanding of how this modification is linked to processes such as the regulation of transcription is still very limited. However, acetylated histones are a characteristic feature of transcriptionally active chromatin (2), and hypoacetylated histones accumulate within transcriptionally silenc...

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“…Certain protein complexes can modify chromatin structure with resultant effects on gene expression (Graessle et al, 2001). A well known mechanism by which chromatin structure can be altered is through the reversible acetylation of lysines within the amino-terminal tails of core histones (Ricci et al, 2002).…”

Section: Role Of Histone Acetylation In Transcriptional Activationmentioning

confidence: 99%

Interaction of maize Opaque-2 and the transcriptional co-activators GCN5 and ADA2, in the modulation of transcriptional activity

et al. 2004

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Maize Opaque-2 (ZmO2), a bZip class transcription factor has been shown to activate the transcription of a series of genes expressed in the maturation phase of endosperm development. Activation requires the presence of one or more enhancer binding sites, which confer the propensity for activation by ZmO2 on heterologous promoters and in heterologous plant cell types, such as tobacco mesophyll protoplasts. The region of ZmO2 required for conferring transcriptional activation has been localised to a stretch of acidic residues in the N-terminal portion of the ZmO2 sequence, which is conserved between O2-related bZip factor sequences. Previously we identified the maize homologues of yeast transcriptional co-activators GCN5 and ADA2 that are implicated in nucleosome modification and transcription. In the present study we have shown that transcriptional modulation by ZmO2 involves the intranuclear interaction of ZmO2 with ZmADA2 and ZmGCN5. Fo¨rster resonance energy transfer (FRET) based techniques have enabled us to estimate the intracellular site of these intermolecular interactions. As a functional readout of these intranuclear interactions, we used the ZmO2 responsive maize b-32 promoter to drive the b-glucuronidase (GUS) in the presence and absence of ZmGCN5 and ZmADA2. Our results suggest that the likely recruitment of ZmADA2 and ZmGCN5 modulates the transactivation of b-32 promoter by ZmO2 and that there may be a competition between ZmGCN5 and ZmO2 for binding to the amino-terminal of ZmADA2. The results may be taken as a paradigm for other processes of transcriptional modulation in planta involving acidic activation domains.

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Histone acetylation: plants and fungi as model systems for the investigation of histone deacetylases

Cited by 38 publications

References 155 publications

Characterization of Inhibitor-Resistant Histone Deacetylase Activity in Plant-Pathogenic Fungi

Characterization of Inhibitor-Resistant Histone Deacetylase Activity in Plant-Pathogenic Fungi

HdaA, a Major Class 2 Histone Deacetylase of Aspergillus nidulans , Affects Growth under Conditions of Oxidative Stress

Interaction of maize Opaque-2 and the transcriptional co-activators GCN5 and ADA2, in the modulation of transcriptional activity

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