A Novel Motif in Fungal Class 1 Histone Deacetylases Is Essential for Growth and Development of Aspergillus
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Acetylation of the N-terminal tails of core histones is an important regulatory mechanism in eukaryotic organisms. In filamentous fungi, little is known about the enzymes that modify histone tails. However, it is increasingly evident that histone deacetylases and histone acetyltransferases are critical factors for the regulation of genes involved in fungal pathogenicity, stress response, and production of secondary metabolites such as antibiotics or fungal toxins. Here, we show that depletion of RpdA, an RPD3-type histone deacetylase of Aspergillus nidulans, leads to a pronounced reduction of growth and sporulation of the fungus. We demonstrate that a so far unnoticed motif in the C terminus of fungal RpdA histone deacetylases is required for the catalytic activity of the enzyme and consequently is essential for the viability of A. nidulans. Moreover, we provide evidence that this motif is also crucial for the survival of other, if not all, filamentous fungi, including pathogens such as Aspergillus fumigatus or Cochliobolus carbonum. Thus, the extended C terminus of RpdA-type enzymes represents a promising target for fungal-specific histone deacetylase-inhibitors that may have potential as novel antifungal compounds with medical and agricultural applications.
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Deletion of rpdA (a class 1 KDAC) was lethal in A. nidulans.
“Interestingly, deletion of rpdA (a class 1 KDAC), whose contribution to KDAC activity is less important, was lethal in A. nidulans, and its repression resulted in growth and conidiation defects that were comparable to the phenotypic consequences of Hsp90 repression in our previous works (7, 12, 41).”
From Identification of a Key Lysine Residue in Heat Shock Protein 90 Required for Azole and Echinocandin Resistance in Aspergillus fumigatus (2014) · cites this paper as [41]
Repression of rpdA resulted in growth and conidiation defects comparable to the phenotypic consequences of Hsp90 repression.
“Interestingly, deletion of rpdA (a class 1 KDAC), whose contribution to KDAC activity is less important, was lethal in A. nidulans, and its repression resulted in growth and conidiation defects that were comparable to the phenotypic consequences of Hsp90 repression in our previous works (7, 12, 41).”
From Identification of a Key Lysine Residue in Heat Shock Protein 90 Required for Azole and Echinocandin Resistance in Aspergillus fumigatus (2014) · cites this paper as [41]
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Cites
The language of covalent histone modifications
Strahl, B. D., & Allis, C. D. (2000) · Nature · doi:10.1038/47412 · Cited by 8,679 · see citing works
Predicting coiled coils from protein sequences.
Lupas, A., Van Dyke, M., & Stock, J. (1991) · Science · doi:10.1126/science.252.5009.1162 · Cited by 3,953 · see citing works
Histone acetylation in chromatin structure and transcription
Grunstein, M. (1997) · Nature · doi:10.1038/38664 · Cited by 2,884 · see citing works
The Genetics of Aspergillus nidulans
Pontecorvo, G., Roper, J. A., Chemmons, L. M., Macdonald, K. D., & Bufton, A. W. J. (1953) · Advances in genetics · doi:10.1016/s0065-2660(08)60408-3 · Cited by 2,305 · see citing works
Chromatin modification and epigenetic reprogramming in mammalian development
Li, E. (2002) · Nature Reviews Genetics · doi:10.1038/nrg887 · Cited by 1,900 · see citing works
Acetylation and deacetylation of non-histone proteins
Glozak, M. A., Sengupta, N., Zhang, X., & Seto, E. (2005) · Gene · doi:10.1016/j.gene.2005.09.010 · Cited by 1,584 · see citing works
Cooperation between Complexes that Regulate Chromatin Structure and Transcription
Narlikar, G. J., Fan, H.-Y., & Kingston, R. E. (2002) · Cell · doi:10.1016/s0092-8674(02)00654-2 · Cited by 1,486 · see citing works
Gregoretti, I., Lee, Y.-M., & Goodson, H. V. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.02.006 · Cited by 1,456 · see citing works
Carrozza, M. J., Li, B., Florens, L. A., Suganuma, T., Swanson, S. K., Lee, K. K., Shia, W.-J., Anderson, S., Yates, J. R., Washburn, M. P., et al. (2005) · Cell · doi:10.1016/j.cell.2005.10.023 · Cited by 1,297 · see citing works
The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men
Yang, X., & Seto, E. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2346 · Cited by 1,239 · see citing works
Histone acetylation and an epigenetic code
Turner, B. M. (2000) · BioEssays · doi:10.1002/1521-1878(200009)22:9 · Cited by 1,214 · see citing works
Meiotic and Mitotic Recombination in Aspergillus and Its Chromosomal Aberrations
Käfer, E. (1977) · Advances in genetics · doi:10.1016/s0065-2660(08)60245-x · Cited by 740 · see citing works
ATP-Dependent Chromatin-Remodeling Complexes
Vignali, M., Hassan, A. H., Neely, K. E., & Workman, J. L. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.6.1899-1910.2000 · Cited by 731 · see citing works
ATP-dependent remodeling and acetylation as regulators of chromatin fluidityPreprint
Kingston, R. E., & Narlikar, G. J. (1999) · Genes & Development · doi:10.1101/gad.13.18.2339 · Cited by 702 · see citing works
Tilburn, J., Sarkar, S., Widdick, D. A., Espeso, E. A., Orejas, M., Mungroo, J., Peñalva, M. A., & Arst, H. N. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07056.x · Cited by 645 · see citing works
Rundlett, S. E., Carmen, A. A., Kobayashi, R., Bavykin, S. G., Turner, B. M., & Grunstein, M. R. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.25.14503 · Cited by 618 · see citing works
Regulation of Secondary Metabolism in Filamentous Fungi
Yu, J., & Keller, N. P. (2005) · Annual Review of Phytopathology · doi:10.1146/annurev.phyto.43.040204.140214 · Cited by 562 · see citing works
Grozinger, C. M., & Schreiber, S. L. (2002) · Chemistry & Biology · doi:10.1016/s1074-5521(02)00092-3 · Cited by 537 · see citing works
Microarray Deacetylation Maps Determine Genome-Wide Functions for Yeast Histone Deacetylases
Robyr, D., Suka, Y., Xénarios, I., Kurdistani, S. K., Wang, A., Suka, N., & Grunstein, M. R. (2002) · Cell · doi:10.1016/s0092-8674(02)00746-8 · Cited by 468 · see citing works
S URFACE A TTACHMENT AND P RE -P ENETRATION S TAGE D EVELOPMENT BY P LANT P ATHOGENIC F UNGI
Tucker, S. L., & Talbot, N. J. (2001) · Annual Review of Phytopathology · doi:10.1146/annurev.phyto.39.1.385 · Cited by 460 · see citing works
Genomewide studies of histone deacetylase function in yeast
Bernstein, B., Tong, J. K., & Schreiber, S. L. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.250477697 · Cited by 419 · see citing works
Histone Deacetylase Activity Regulates Chemical Diversity in Aspergillus
Shwab, E. K., Bok, J. W., Tribus, M., Galehr, J., Graessle, S., & Keller, N. P. (2007) · Eukaryotic Cell · doi:10.1128/ec.00186-07 · Cited by 414 · see citing works
Self-citationTurner, B. M. (2007) · Nature Cell Biology · doi:10.1038/ncb0107-2 · Cited by 392 · see citing works
Chromatin remodeling by ATP‐dependent molecular machines
Lusser, A., & Kadonaga, J. T. (2003) · BioEssays · doi:10.1002/bies.10359 · Cited by 351 · see citing works
25 years after the nucleosome model: chromatin modifications
Wu, J. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01718-7 · Cited by 342 · see citing works
Vidal, M., & Gaber, R. F. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.12.6317 · Cited by 321 · see citing works
The MAPK Hog1 recruits Rpd3 histone deacetylase to activate osmoresponsive genes
de Nadal, E., Zapater, M., Alepuz, P. M., Sumoy, L., Martín, G. M., & Posas, F. (2004) · Nature · doi:10.1038/nature02258 · Cited by 316 · see citing works
Genome-wide patterns of histone modifications in yeast
Millar, C. B., & Grunstein, M. R. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1986 · Cited by 286 · see citing works
Requirement of Hos2 Histone Deacetylase for Gene Activity in Yeast
Wang, A., Kurdistani, S. K., & Grunstein, M. R. (2002) · Science · doi:10.1126/science.1077790 · Cited by 272 · see citing works
The Constantly Changing Face of Chromatin
Vaquero, A., Loyola, A., & Reinberg, D. (2003) · Science of Aging Knowledge Environment · doi:10.1126/sageke.2003.14.re4 · Cited by 236 · see citing works
Brakhage, A. A. (2005) · Current Drug Targets · doi:10.2174/138945005774912717 · Cited by 191 · see citing works
Nicolas, E., Yamada, T., Cam, H. P., FitzGerald, P. C., Kobayashi, R., & Grewal, S. I. S. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1239 · Cited by 187 · see citing works
Histone modifications and chromatin dynamics: a focus on filamentous fungi
Brosch, G., Loidl, P., & Graessle, S. (2008) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2007.00100.x · Cited by 174 · see citing works
Self-citationGenome wide analysis of nucleosome density histone acetylation and HDAC function in fission yeast
Wirén, M., Silverstein, R. A., Sinha, I., Walfridsson, J., Lee, H.-M., Laurenson, P., Pillus, L., Robyr, D., Grunstein, M. R., & Ekwall, K. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600758 · Cited by 155 · see citing works
Lee, I., Oh, J., Shwab, E. K., Dagenais, T. R. T., Andes, D. R., & Keller, N. P. (2009) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2009.06.007 · Cited by 148 · see citing works
Cloning of the riboB locus of Aspergillus nidulans
Oakley, C. E., Weil, C. F., Kretz, P. L., & Oakley, B. R. (1987) · Gene · doi:10.1016/0378-1119(87)90019-9 · Cited by 143 · see citing works
Global Effects on Gene Expression in Fission Yeast by Silencing and RNA Interference Machineries
Hansen, K., Burns, G., Mata, J., Volpe, T. A., Martienssen, R. A., Bähler, J., & Thon, G. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.2.590-601.2005 · Cited by 137 · see citing works
Stable incorporation of sequence specific repressors Ash1 and Ume6 into the Rpd3L complex
Carrozza, M. J., Florens, L. A., Swanson, S. K., Shia, W.-J., Anderson, S., Yates, J. R., Washburn, M. P., & Workman, J. L. (2005) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/j.bbaexp.2005.09.005 · Cited by 132 · see citing works
Srikantha, T., Tsai, L., Daniels, K. G., Klar, A. J. S., & Soll, D. R. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.15.4614-4625.2001 · Cited by 132 · see citing works
Zadra, I., Abt, B., Parson, W., & Haas, H. (2000) · Applied and Environmental Microbiology · doi:10.1128/aem.66.11.4810-4816.2000 · Cited by 131 · see citing works
Self-citationEthanol catabolism in Aspergillus nidulans: A model system for studying gene regulation
Felenbok, B., Flipphi, M. J. A., & Nikolaev, I. (2001) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(01)69047-0 · Cited by 130 · see citing works
Aspergillus fumigatus : Growth and virulence
Rhodes, J. C. (2006) · Medical Mycology · doi:10.1080/13693780600779419 · Cited by 120 · see citing works
The Nucleosome: A Powerful Regulator of Transcription
Wolffe, A. P., & Kurumizaka, H. (1998) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(08)60832-6 · Cited by 114 · see citing works
The art and design of genetic screens: filamentous fungi
Casselton, L. A., & Zolan, M. E. (2002) · Nature Reviews Genetics · doi:10.1038/nrg889 · Cited by 108 · see citing works
Histone deacetylases: salesmen and customers in the post‐translational modification market
Brandl, A., Heinzel, T., & Krämer, O. H. (2009) · Biology of the Cell · doi:10.1042/bc20080158 · Cited by 107 · see citing works
Histone deacetylases in fungi: novel members, new facts
Trojer, P. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg473 · Cited by 86 · see citing works
Self-citationThe Sir2 protein family: A novel deacetylase for gene silencing and more
Shore, D. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.011506198 · Cited by 82 · see citing works
Panozzo, C., Cornillot, E., & Felenbok, B. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.11.6367 · Cited by 75 · see citing works
Baidyaroy, D., Brosch, G., Ahn, J., Graessle, S., Wegener, S., Tonukari, N. J., Caballero, O., Loidl, P., & Walton, J. D. (2001) · The Plant Cell · doi:10.1105/tpc.010168 · Cited by 70 · see citing works
Self-citationTribus, M., Galehr, J., Trojer, P., Brosch, G., Loidl, P., Marx, F., Haas, H., & Graessle, S. (2005) · Eukaryotic Cell · doi:10.1128/ec.4.10.1736-1745.2005 · Cited by 67 · see citing works
Self-citationMolecular characterization of the Aspergillus nidulans yA locus.
O'Hara, E. B., & Timberlake, W. E. (1989) · Genetics · doi:10.1093/genetics/121.2.249 · Cited by 60 · see citing works
The Pharmaceutical Potential of Histone Deacetylase Inhibitors
Elaut, G., Rogiers, V., & Vanhaecke, T. (2007) · Current Pharmaceutical Design · doi:10.2174/138161207781663064 · Cited by 59 · see citing works
Korber, P., & Hörz, W. (2004) · Cell · doi:10.1016/s0092-8674(04)00296-x · Cited by 59 · see citing works
Characterization of two putative histone deacetylase genes from Aspergillus nidulans
Graessle, S., Dangl, M., Haas, H., Mair, K., Trojer, P., Brandtner, E., Walton, J. D., Loidl, P., & Brosch, G. (2000) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(00)00093-2 · Cited by 48 · see citing works
Self-citationHistone acetylation: plants and fungi as model systems for the investigation of histone deacetylases
Graessle, S., Loidl, P., & Brosch, G. (2001) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000894 · Cited by 45 · see citing works
Self-citationCloning and structural organization of a xylanase-encoding gene from Penicillium chrysogenum
Haas, H., Friedlin, E., Stöffler, G., & Redl, B. (1993) · Gene · doi:10.1016/0378-1119(93)90372-a · Cited by 41 · see citing works
Self-citationRegulated system for heterologous gene expression in Penicillium chrysogenum
Graessle, S., Haas, H., Friedlin, E., Kürnsteiner, H., Stöffler, G., & Redl, B. (1997) · Applied and Environmental Microbiology · doi:10.1128/aem.63.2.753-756.1997 · Cited by 27 · see citing works
Self-citationAnalysis of Genome-Wide Histone Acetylation State and Enzyme Binding Using DNA Microarrays
Robyr, D., Kurdistani, S. K., & GRUNSTEIN, M. M. (2003) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(03)76019-4 · Cited by 24 · see citing works
An Inhibitor-Resistant Histone Deacetylase in the Plant Pathogenic Fungus Cochliobolus carbonum
Brosch, G., Dangl, M., Graessle, S., Loidl, A., Trojer, P., Brandtner, E., Mair, K., Walton, J. D., Baidyaroy, D., & Loidl, P. (2001) · Biochemistry · doi:10.1021/bi010508u · Cited by 19 · see citing works
Self-citationColina, A. R., & Young, D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m511561200 · Cited by 18 · see citing works
Ruault, M., & Pillus, L. (2006) · Genetics · doi:10.1534/genetics.106.059873 · Cited by 18 · see citing works
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Pfannenstiel, B. T., & Keller, N. P. (2019) · Biotechnology Advances · doi:10.1016/j.biotechadv.2019.02.001 · Cited by 168 · see citing works
Li, Y., Wang, C., Liu, W., Wang, G., Kang, Z., Kistler, H. C., & Xu, J. (2010) · Molecular Plant-Microbe Interactions · doi:10.1094/mpmi-10-10-0233 · Cited by 104 · see citing works
Albright, J. C., Henke, M. T., Soukup, A. A., McClure, R. A., Thomson, R. J., Keller, N. P., & Kelleher, N. L. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00025 · Cited by 98 · see citing works
Pillay, L. C., Nekati, L., Makhwitine, J. P., & Ndlovu, S. I. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.815008 · Cited by 82 · see citing works
Epigenetic mechanisms of drug resistance in fungi
Chang, Z., Yadav, V., Lee, S. C., & Heitman, J. (2019) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2019.103253 · Cited by 81 · see citing works
Cánovas, D., Marcos, A. T., Gacek, A., Ramos, M. S., Gutiérrez, G., Reyes-Domínguez, Y., & Strauss, J. (2014) · Genetics · doi:10.1534/genetics.114.165688 · Cited by 75 · see citing works
Trichoderma Histone Deacetylase HDA-2 Modulates Multiple Responses in Arabidopsis
Estrada‐Rivera, M., Rebolledo‐Prudencio, O. G., Pérez-Robles, D. A., Rocha-Medina, M. D. C., González-López, M. D. C., & Casas‐Flores, S. (2019) · PLANT PHYSIOLOGY · doi:10.1104/pp.18.01092 · Cited by 75 · see citing works
Lamoth, F., Juvvadi, P. R., Soderblom, E. J., Moseley, M. A., Asfaw, Y. G., & Steinbach, W. J. (2014) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02286-13 · Cited by 74 · see citing works
Kawauchi, M., Nishiura, M., & Iwashita, K. (2013) · Eukaryotic Cell · doi:10.1128/ec.00003-13 · Cited by 74 · see citing works
Post‐translational modifications drive secondary metabolite biosynthesis in Aspergillus : a review
Yang, K., Tian, J., & Keller, N. P. (2022) · Environmental Microbiology · doi:10.1111/1462-2920.16034 · Cited by 61 · see citing works
Histone deacetylase inhibition as an alternative strategy against invasive aspergillosis
Lamoth, F., Juvvadi, P. R., & Steinbach, W. J. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00096 · Cited by 61 · see citing works
Small Chemical Chromatin Effectors Alter Secondary Metabolite Production in Aspergillus clavatus
Zutz, C., Gacek‐Matthews, A., Sulyok, M., Wagner, M., Strauss, J., & Rychli, K. (2013) · Toxins · doi:10.3390/toxins5101723 · Cited by 59 · see citing works
Karahoda, B., Pardeshi, L. A., Ulaş, M., Dong, Z., Shirgaonkar, N., Guo, S., Wang, F., Tan, K., Bayram, Ö. S., Bauer, I., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac744 · Cited by 53 · see citing works
Self-citationPidroni, A., Faber, B., Brosch, G., Bauer, I., & Graessle, S. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.02212 · Cited by 48 · see citing works
Self-citationA Class 1 Histone Deacetylase with Potential as an Antifungal Target
Bauer, I., Varadarajan, D., Pidroni, A., Gross, S., Vergeiner, S., Faber, B., Hermann, M., Tribus, M., Brosch, G., & Graessle, S. (2016) · mBio · doi:10.1128/mbio.00831-16 · Cited by 49 · see citing works
Self-citationHydrolase Controls Cellular NAD, Sirtuin, and Secondary Metabolites
Shimizu, M., Masuo, S., Fujita, T., Doi, Y., Kamimura, Y., & Takaya, N. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00032-12 · Cited by 47 · see citing works
Lan, H., Wu, L., Sun, R., Keller, N. P., Yang, K., Ye, L., He, S., Zhang, F., & Wang, S. (2019) · Molecular Plant-Microbe Interactions · doi:10.1094/mpmi-01-19-0033-r · Cited by 47 · see citing works
H2B- and H3-Specific Histone Deacetylases Are Required for DNA Methylation in Neurospora crassa
Smith, K., Dobosy, J. R., Reifsnyder, J. E., Rountree, M. R., Anderson, D. C., Green, G. R., & Selker, E. U. (2010) · Genetics · doi:10.1534/genetics.110.123315 · Cited by 44 · see citing works
Chen, S. C.-A., Lewis, R. E., & Kontoyiannis, D. P. (2011) · Virulence · doi:10.4161/viru.2.4.16764 · Cited by 41 · see citing works
Maeda, K., Izawa, M., Nakajima, Y., Jin, Q., Hirose, T., Nakamura, T. Y., Koshino, H., Kanamaru, K., Ohsato, S., Kamakura, T., et al. (2017) · Letters in Applied Microbiology · doi:10.1111/lam.12797 · Cited by 41 · see citing works
Cai, Q., Wang, Z., Shao, W., Ying, S., & Feng, M. (2018) · Environmental Microbiology · doi:10.1111/1462-2920.14100 · Cited by 38 · see citing works
Protein Acetylation/Deacetylation: A Potential Strategy for Fungal Infection Control
Chen, J.-Z., Liu, Q., Zeng, L., & Huang, X. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.574736 · Cited by 35 · see citing works
Li, X., Pan, L., Wang, B., & Pan, L. (2019) · Toxins · doi:10.3390/toxins11090520 · Cited by 34 · see citing works
Lee, S. H., Farh, M. E.-A., Lee, J., Oh, Y. T., Cho, E., Park, J., Son, H., & Jeon, J. (2021) · mBio · doi:10.1128/mbio.02600-21 · Cited by 32 · see citing works
The Lysine Deacetylase RpdA Is Essential for Virulence in Aspergillus fumigatus
Bauer, I., Misslinger, M., Shadkchan, Y., Dietl, A., Petzer, V., Orasch, T., Abt, B., Graessle, S., Osherov, N., & Haas, H. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.02773 · Cited by 30 · see citing works
Self-citationKawauchi, M., & Iwashita, K. (2014) · Journal of Bioscience and Bioengineering · doi:10.1016/j.jbiosc.2014.02.004 · Cited by 30 · see citing works
Osorio-Concepción, M., Cristóbal‐Mondragón, G. R., Gutiérrez–Medina, B., & Casas‐Flores, S. (2016) · Applied and Environmental Microbiology · doi:10.1128/aem.02922-16 · Cited by 29 · see citing works
BcRPD3-Mediated Histone Deacetylation Is Involved in Growth and Pathogenicity of Botrytis cinerea
Zhang, N., Yang, Z., Zhang, Z., & Liang, W. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.01832 · Cited by 28 · see citing works
Liu, S., Wang, Q., Liu, N., Luo, H., He, C., & An, B. (2022) · Phytopathology Research · doi:10.1186/s42483-022-00126-0 · Cited by 24 · see citing works
Aspergillus nidulans galactofuranose biosynthesis affects antifungal drug sensitivity
Alam, M. K., El-Ganiny, A. M., Afroz, S., Sanders, D. A. R., Liu, J., & Kaminskyj, S. G. W. (2012) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2012.08.010 · Cited by 24 · see citing works
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Smith, K., Phatale, P. A., Bredeweg, E., Connolly, L., Pomraning, K., & Freitag, M. (2012) · Wiley-VCH eBooks · doi:10.1002/3527600906.mcb.201100035 · Cited by 23 · see citing works
Epigenetic and Posttranslational Modifications in Regulating the Biology of Aspergillus Species
Nie, X., Li, B., & Wang, S. (2018) · Advances in applied microbiology · doi:10.1016/bs.aambs.2018.05.004 · Cited by 21 · see citing works
Karahoda, B., Pfannenstiel, B. T., Bayram, Ö. S., Dong, Z., Wong, K. H., Fleming, A. B., Keller, N. P., & Bayram, Ö. (2023) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2023.103836 · Cited by 19 · see citing works
Yap, A., Glarcher, I., Misslinger, M., & Haas, H. (2022) · Metabolic Engineering Communications · doi:10.1016/j.mec.2022.e00214 · Cited by 17 · see citing works
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Liu, L., Wang, B., Duan, G., Wang, J., Pan, Z., Ou, M., Bai, X., Peiying, W., Zhao, D., Nan, N., et al. (2023) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.3c01782 · Cited by 16 · see citing works
Zheng, Y., Huang, Y., Mao, Z., & Shao, Y. (2021) · Food Control · doi:10.1016/j.foodcont.2021.108457 · Cited by 15 · see citing works
Long, Z., Peiying, W., Yu, Q., Wang, B., Li, D., Yang, C., Liu, L., Duan, G., & Sun, W. (2024) · Phytopathology Research · doi:10.1186/s42483-024-00230-3 · Cited by 11 · see citing works
Epigenetics of Fungal Secondary Metabolism Related Genes
Wu, M.-Y., & Yu, J. (2015) · Fungal biology · doi:10.1007/978-1-4939-2531-5_3 · Cited by 12 · see citing works
The histone code of the fungal genus Aspergillus uncovered by evolutionary and proteomic analyses
Zhang, X., Noberini, R., Bonaldi, T., Collemare, J., & Seidl, M. F. (2022) · Microbial Genomics · doi:10.1099/mgen.0.000856 · Cited by 11 · see citing works
Anjo, S. I., Figueiredo, F., Fernandes, R., Manadas, B. J., & Oliveira, M. T. D. S. (2017) · Journal of Proteomics · doi:10.1016/j.jprot.2017.03.021 · Cited by 11 · see citing works
RcLS2F – A Novel Fungal Class 1 KDAC Co-repressor Complex in Aspergillus nidulans
Bauer, I., Gross, S., Merschak, P., Kremser, L., Karahoda, B., Bayram, Ö. S., Abt, B., Binder, U., Gsaller, F., Lindner, H. H., et al. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.00043 · Cited by 11 · see citing works
Self-citationLysine acetylation as drug target in fungi: an underexplored potential in Aspergillus spp.
Wassano, N. S., Leite, A. B., Reichert‐Lima, F., Schreiber, A. Z., Moretti, N. S., & Damásio, A. (2020) · Brazilian Journal of Microbiology · doi:10.1007/s42770-020-00253-w · Cited by 10 · see citing works
Sirtuin E deacetylase is required for full virulence of Aspergillus fumigatus
Wassano, N. S., Silva, G. B., Reis, A. H., Gerhardt, J. A., Antoniel, E. P., Akiyama, D. Y., Rezende, C. P., Neves, L. X., Vasconcelos, E. J. R., de Figueiredo, F. L., et al. (2024) · Communications Biology · doi:10.1038/s42003-024-06383-3 · Cited by 10 · see citing works
8 Coordination of Fungal Secondary Metabolism and Development
Gerke, J., Köhler, A. M., Meister, C., Thieme, K. G., Amoedo, H., & Braus, G. H. (2020) · Springer eBooks · doi:10.1007/978-3-030-49924-2_8 · Cited by 9 · see citing works
Fungal Lysine Deacetylases in Virulence, Resistance, and Production of Small Bioactive Compounds
Bauer, I., & Graessle, S. (2021) · Genes · doi:10.3390/genes12101470 · Cited by 10 · see citing works
Self-citationNishida, H., Motoyama, T., Suzuki, Y., Yamamoto, S., Aburatani, H., & Osada, H. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009916 · Cited by 9 · see citing works
Speckbacher, V., Flatschacher, D., Martini-Lösch, N., Ulbrich, L., Baldin, C., Bauer, I., Ruzsányi, V., & Zeilinger, S. (2024) · Microbiology Spectrum · doi:10.1128/spectrum.03097-23 · Cited by 9 · see citing works
Self-citationAnalysis of lysine acetylation in tomato spot wilt virus infection in Nicotiana benthamiana
Gong, Y., Li, Y., Liu, D., Jiang, L., Liang, H., Wu, Y., Wang, F., & Yang, J. (2023) · Frontiers in Microbiology · doi:10.3389/fmicb.2023.1046163 · Cited by 9 · see citing works
5 Fungal Chromatin and Its Role in Regulation of Gene Expression
Freitag, M. (2014) · Springer eBooks · doi:10.1007/978-3-642-45218-5_5 · Cited by 8 · see citing works
Li, Y., Song, Z., Wang, E., Dong, L., Bai, J., Wang, D., Zhu, J., & Zhang, C. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.980615 · Cited by 7 · see citing works
Shanmugam, G., Kim, T., & Jeon, J. (2019) · Molecules · doi:10.3390/molecules24112075 · Cited by 6 · see citing works
Bauer, I., Pidroni, A., Bayram, Ö., Brosch, G., & Graessle, S. (2019) · Journal of Visualized Experiments · doi:10.3791/59527 · Cited by 5 · see citing works
Self-citation(2013) · International Journal of Biosciences (IJB) · doi:10.12692/ijb/3.12.9-16 · Cited by 3 · see citing works
Histone acetyltransferases and histone deacetylases of trichoderma
Sharma, V., & Salwan, R. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-91734-6.00008-9 · Cited by 2 · see citing works
Ries, L. N. A. (2013) · Nottingham ePrints (University of Nottingham) · Cited by 2 · see citing works
Chapter 10. Epigenetic Approaches to Natural Product Synthesis in Fungi
Soukup, A. A., & Keller, N. P. (2012) · Royal Society of Chemistry eBooks · doi:10.1039/9781849733618-00198 · Cited by 2 · see citing works
Deacetylation by sirtuins is important for Aspergillus fumigatus pathogenesis and virulencePreprint
Wassano, N. S., da Silva, G. B., Reis, A. H., Gerhardt, J. A., Antoniel, E. P., Akiyama, D. Y., Rezende, C. P., Neves, L. X., Vasconcelos, E. J. R., de Figueiredo, F. L., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.25.558961 · Cited by 1 · see citing works
The Aspergillus nidulans Galf biosynthesis pathway is a promising drug target
El-Ganiny, A. M. (2011) · University Library - University of Saskatchewan (University of Saskatchewan)
Jäger, N., Rosin, M., Stroe, M. C., Brakhage, A. A., & Heinzel, T. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.12.05.569573
Liu, S., Wang, Q., Liu, N., Luo, H., He, C., & An, B. (2022) · Figshare · doi:10.6084/m9.figshare.20004761
Alam, K. (2014) · University Library - University of Saskatchewan (University of Saskatchewan)
Liu, S., Wang, Q., Liu, N., Luo, H., He, C., & An, B. (2022) · Figshare · doi:10.6084/m9.figshare.20004764
Long, Z., Peiying, W., Yu, Q., Wang, B., Li, D., Yang, C., Liu, L., Duan, G., & Sun, W. (2024) · Figshare · doi:10.6084/m9.figshare.26677670
Long, Z., Peiying, W., Yu, Q., Wang, B., Li, D., Yang, C., Liu, L., Duan, G., & Sun, W. (2024) · Figshare · doi:10.6084/m9.figshare.26677673
Liao, H.-X., Wen, J.-R., Shi, H.-M., Cun, H.-Q., Hong, Y.-J., Hu, Z.-F., Xu, F.-R., Noiprasert, S., Apiwongsrichai, K., Liu, X.-Y., et al. (2026) · IMA Fungus · doi:10.3897/imafungus.17.168980
- Authors
- Tribus, M., Bauer, I., Galehr, J., Rieser, G., Trojer, P., Brosch, G., Loidl, P., Haas, H., & Graessle, S.
- Affiliations
- Innsbruck Medical University (AT)
- Corresponding author
- Graessle, Stefan
- Venue
- Molecular Biology of the Cell
- Published
- 2010-01-15
- Volume
- 21
- Issue
- 2
- Pages
- 345-353
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- PMC
- PMC2808227
- OpenAlex
- W2118449874
- Cited by
- 63
- References
- 61
- Citations by year
- 2026: 1 · 2024: 4 · 2023: 6 · 2022: 8 · 2021: 3 · 2020: 5 · 2019: 8 · 2018: 3 · 2017: 2 · 2016: 2 · 2015: 3 · 2014: 5 · 2013: 4 · 2012: 4
- FWCI
- 1.21
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular Biology of the Cell (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- histone deacetylase, Aspergillus nidulans, Aspergillus fumigatus, Cochliobolus carbonum, histone acetylation, C-terminal motif, catalytic activity, sporulation, fungal growth, antifungal drug targets, histone deacetylase inhibitors, filamentous fungi
- MeSH terms
- Acetylation, Amino Acid Sequence, Aspergillus fumigatus, Aspergillus nidulans, Fungal Proteins, Genotype, Histone Deacetylases, Histones, Molecular Sequence Data, Phenotype, Structure-Activity Relationship, Transcription, Genetic, Conserved Sequence, Amino Acid Motifs
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