The Fng3 ING protein regulates H3 acetylation and H4 deacetylation by interacting with two distinct histone-modifying complexes
© 2022 The Authors. New Phytologist © 2022 New Phytologist Foundation.
| Veröffentlicht in: | The New phytologist. - 1979. - 235(2022), 6 vom: 01. Sept., Seite 2350-2364 |
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| Weitere Verfasser: | , , , , , , , , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2022
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| Zugriff auf das übergeordnete Werk: | The New phytologist |
| Schlagworte: | Journal Article Fusarium graminearum ING protein histone acetylation histone deacetylation pathogenesis phytopathogenic fungus wheat head blight Fungal Proteins Histones mehr... |
| Zusammenfassung: | © 2022 The Authors. New Phytologist © 2022 New Phytologist Foundation. The steady-state level of histone acetylation is maintained by histone acetyltransferase (HAT) and histone deacetylase (HDAC) complexes. INhibitor of Growth (ING) proteins are key components of the HAT or HDAC complexes but their relationship with other components and roles in phytopathogenic fungi are not well-characterized. Here, the FNG3 ING gene was functionally characterized in the wheat head blight fungus Fusarium graminearum. Deletion of FNG3 results in defects in fungal development and pathogenesis. Unlike other ING proteins that are specifically associated with distinct complexes, Fng3 was associated with both NuA3 HAT and FgRpd3 HDAC complexes to regulate H3 acetylation and H4 deacetylation. Whereas FgNto1 mediates the FgSas3-Fng3 interaction in the NuA3 complex, Fng3 interacted with the C-terminal region of FgRpd3 that is present in Rpd3 orthologs from filamentous fungi but absent in yeast Rpd3. The intrinsically disordered regions in the C-terminal tail of FgRpd3 underwent phase separation, which was important for its interaction with Fng3. Furthermore, the ING domain of Fng3 is responsible for its specificities in protein-protein interactions and functions. Taken together, Fng3 is involved in the dynamic regulation of histone acetylation by interacting with two histone modification complexes, and is important for fungal development and pathogenicity |
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| Beschreibung: | Date Completed 19.08.2022 Date Revised 25.05.2023 published: Print-Electronic RefSeq: SRR17659995, SRR17660003, SRR19214415, SRR19214418, SRR19414282, SRR19414283 ErratumIn: New Phytol. 2023 Jul;239(2):807-809. - PMID 37227125 Citation Status MEDLINE |
| ISSN: | 1469-8137 |
| DOI: | 10.1111/nph.18294 |