A missense mutation in the Sin3 subunit of Rpd3 histone deacetylase complex bypasses the requirement for FNG1 in wheat scab fungus
The Rpd3 histone deacetylase complex is a multiple-subunit complex that mediates the regulation of chromatin accessibility and gene expression. Sin3, the largest subunit of Rpd3 complex, is conserved in a broad range of eukaryotes. Despite being a molecular scaffold for complex assembly, the functio...
Saved in:
| Main Authors: | , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
KeAi Communications Co., Ltd.
2025-08-01
|
| Series: | Journal of Integrative Agriculture |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2095311924000066 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1849247582519296000 |
|---|---|
| author | Huaijian Xu Ruoxuan Jiang Xianhui Fu Qinhu Wang Yutong Shi Xiaofei Zhao Cong Jiang Hang Jiang |
| author_facet | Huaijian Xu Ruoxuan Jiang Xianhui Fu Qinhu Wang Yutong Shi Xiaofei Zhao Cong Jiang Hang Jiang |
| author_sort | Huaijian Xu |
| collection | DOAJ |
| description | The Rpd3 histone deacetylase complex is a multiple-subunit complex that mediates the regulation of chromatin accessibility and gene expression. Sin3, the largest subunit of Rpd3 complex, is conserved in a broad range of eukaryotes. Despite being a molecular scaffold for complex assembly, the functional sites and mechanism of action of Sin3 remain unexplored. In this study, we functionally characterized a glutamate residue (E810) in FgSin3, the ortholog of yeast Sin3 in Fusarium graminearum (known as wheat scab fungus). Our findings indicate that E810 was important for the functions of FgSin3 in regulating vegetative growth, sexual reproduction, wheat infection, and DON biosynthesis. Furthermore, the E810K missense mutation restored the reduced H4 acetylation caused by the deletion of FNG1, the ortholog of the human inhibitor of growth (ING1) gene in F. graminearum. Correspondingly, the defects of the fng1 mutant were also partially rescued by the E810K mutation in FgSin3. Sequence alignment and evolutionary analysis revealed that E810 residue is well-conserved in fungi, animals, and plants. Based on Alphafold2 structure modeling, E810 localized on the FgRpd3–FgSin3 interface for the formation of a hydrogen bond with FgRpd3. Mutation of E810 disrupts the hydrogen bond and likely affects the FgRpd3–FgSin3 interaction. Taken together, E810 of FgSin3 is functionally associated with Fng1 in the regulation of H4 acetylation and related biological processes, probably by affecting the assembly of the Rpd3 complex. |
| format | Article |
| id | doaj-art-3ca234fc834940dfabe7dc7f18758ecd |
| institution | Kabale University |
| issn | 2095-3119 |
| language | English |
| publishDate | 2025-08-01 |
| publisher | KeAi Communications Co., Ltd. |
| record_format | Article |
| series | Journal of Integrative Agriculture |
| spelling | doaj-art-3ca234fc834940dfabe7dc7f18758ecd2025-08-20T03:58:10ZengKeAi Communications Co., Ltd.Journal of Integrative Agriculture2095-31192025-08-012483087309410.1016/j.jia.2024.01.006A missense mutation in the Sin3 subunit of Rpd3 histone deacetylase complex bypasses the requirement for FNG1 in wheat scab fungusHuaijian Xu0Ruoxuan Jiang1Xianhui Fu2Qinhu Wang3Yutong Shi4Xiaofei Zhao5Cong Jiang6Hang Jiang7State Key Laboratory for Crop Stress Resistance and High-Efficiency Production, College of Plant Protection, Northwest A&F University, Yangling 712100, ChinaState Key Laboratory for Crop Stress Resistance and High-Efficiency Production, College of Plant Protection, Northwest A&F University, Yangling 712100, ChinaState Key Laboratory for Crop Stress Resistance and High-Efficiency Production, College of Plant Protection, Northwest A&F University, Yangling 712100, ChinaState Key Laboratory for Crop Stress Resistance and High-Efficiency Production, College of Plant Protection, Northwest A&F University, Yangling 712100, ChinaState Key Laboratory for Crop Stress Resistance and High-Efficiency Production, College of Plant Protection, Northwest A&F University, Yangling 712100, ChinaState Key Laboratory for Crop Stress Resistance and High-Efficiency Production, College of Plant Protection, Northwest A&F University, Yangling 712100, ChinaState Key Laboratory for Crop Stress Resistance and High-Efficiency Production, College of Plant Protection, Northwest A&F University, Yangling 712100, China; Correspondence Cong JiangShandong Key Laboratory for Green Prevention and Control of Agricultural Pests, Institute of Plant Protection, Shandong Academy of Agricultural Sciences, Jinan 250100, China; Correspondence Hang JiangThe Rpd3 histone deacetylase complex is a multiple-subunit complex that mediates the regulation of chromatin accessibility and gene expression. Sin3, the largest subunit of Rpd3 complex, is conserved in a broad range of eukaryotes. Despite being a molecular scaffold for complex assembly, the functional sites and mechanism of action of Sin3 remain unexplored. In this study, we functionally characterized a glutamate residue (E810) in FgSin3, the ortholog of yeast Sin3 in Fusarium graminearum (known as wheat scab fungus). Our findings indicate that E810 was important for the functions of FgSin3 in regulating vegetative growth, sexual reproduction, wheat infection, and DON biosynthesis. Furthermore, the E810K missense mutation restored the reduced H4 acetylation caused by the deletion of FNG1, the ortholog of the human inhibitor of growth (ING1) gene in F. graminearum. Correspondingly, the defects of the fng1 mutant were also partially rescued by the E810K mutation in FgSin3. Sequence alignment and evolutionary analysis revealed that E810 residue is well-conserved in fungi, animals, and plants. Based on Alphafold2 structure modeling, E810 localized on the FgRpd3–FgSin3 interface for the formation of a hydrogen bond with FgRpd3. Mutation of E810 disrupts the hydrogen bond and likely affects the FgRpd3–FgSin3 interaction. Taken together, E810 of FgSin3 is functionally associated with Fng1 in the regulation of H4 acetylation and related biological processes, probably by affecting the assembly of the Rpd3 complex.http://www.sciencedirect.com/science/article/pii/S2095311924000066histone acetylationING proteinphytopathogenRpd3 histone deacetylase complex |
| spellingShingle | Huaijian Xu Ruoxuan Jiang Xianhui Fu Qinhu Wang Yutong Shi Xiaofei Zhao Cong Jiang Hang Jiang A missense mutation in the Sin3 subunit of Rpd3 histone deacetylase complex bypasses the requirement for FNG1 in wheat scab fungus Journal of Integrative Agriculture histone acetylation ING protein phytopathogen Rpd3 histone deacetylase complex |
| title | A missense mutation in the Sin3 subunit of Rpd3 histone deacetylase complex bypasses the requirement for FNG1 in wheat scab fungus |
| title_full | A missense mutation in the Sin3 subunit of Rpd3 histone deacetylase complex bypasses the requirement for FNG1 in wheat scab fungus |
| title_fullStr | A missense mutation in the Sin3 subunit of Rpd3 histone deacetylase complex bypasses the requirement for FNG1 in wheat scab fungus |
| title_full_unstemmed | A missense mutation in the Sin3 subunit of Rpd3 histone deacetylase complex bypasses the requirement for FNG1 in wheat scab fungus |
| title_short | A missense mutation in the Sin3 subunit of Rpd3 histone deacetylase complex bypasses the requirement for FNG1 in wheat scab fungus |
| title_sort | missense mutation in the sin3 subunit of rpd3 histone deacetylase complex bypasses the requirement for fng1 in wheat scab fungus |
| topic | histone acetylation ING protein phytopathogen Rpd3 histone deacetylase complex |
| url | http://www.sciencedirect.com/science/article/pii/S2095311924000066 |
| work_keys_str_mv | AT huaijianxu amissensemutationinthesin3subunitofrpd3histonedeacetylasecomplexbypassestherequirementforfng1inwheatscabfungus AT ruoxuanjiang amissensemutationinthesin3subunitofrpd3histonedeacetylasecomplexbypassestherequirementforfng1inwheatscabfungus AT xianhuifu amissensemutationinthesin3subunitofrpd3histonedeacetylasecomplexbypassestherequirementforfng1inwheatscabfungus AT qinhuwang amissensemutationinthesin3subunitofrpd3histonedeacetylasecomplexbypassestherequirementforfng1inwheatscabfungus AT yutongshi amissensemutationinthesin3subunitofrpd3histonedeacetylasecomplexbypassestherequirementforfng1inwheatscabfungus AT xiaofeizhao amissensemutationinthesin3subunitofrpd3histonedeacetylasecomplexbypassestherequirementforfng1inwheatscabfungus AT congjiang amissensemutationinthesin3subunitofrpd3histonedeacetylasecomplexbypassestherequirementforfng1inwheatscabfungus AT hangjiang amissensemutationinthesin3subunitofrpd3histonedeacetylasecomplexbypassestherequirementforfng1inwheatscabfungus AT huaijianxu missensemutationinthesin3subunitofrpd3histonedeacetylasecomplexbypassestherequirementforfng1inwheatscabfungus AT ruoxuanjiang missensemutationinthesin3subunitofrpd3histonedeacetylasecomplexbypassestherequirementforfng1inwheatscabfungus AT xianhuifu missensemutationinthesin3subunitofrpd3histonedeacetylasecomplexbypassestherequirementforfng1inwheatscabfungus AT qinhuwang missensemutationinthesin3subunitofrpd3histonedeacetylasecomplexbypassestherequirementforfng1inwheatscabfungus AT yutongshi missensemutationinthesin3subunitofrpd3histonedeacetylasecomplexbypassestherequirementforfng1inwheatscabfungus AT xiaofeizhao missensemutationinthesin3subunitofrpd3histonedeacetylasecomplexbypassestherequirementforfng1inwheatscabfungus AT congjiang missensemutationinthesin3subunitofrpd3histonedeacetylasecomplexbypassestherequirementforfng1inwheatscabfungus AT hangjiang missensemutationinthesin3subunitofrpd3histonedeacetylasecomplexbypassestherequirementforfng1inwheatscabfungus |