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Updated: Oct 19, 2025

Genome-wide Analysis of Histone Modifications Distribution using the Chromatin Immunoprecipitation Sequencing Method in Magnaporthe oryzae
Published on: June 2, 2021
Fusarium BP1 is a reader of H3K27 methylation
Guangfei Tang1,2, Jianlong Yuan3, Jing Wang1
1State Key Laboratory of Rice Biology, Key Laboratory of Molecular Biology of Crop Pathogens and Insects, Institute of Biotechnology, Zhejiang University, Hangzhou 310058, China.
Abstract:
Histone H3 lysine 27 methylation catalyzed by polycomb repressive complex 2 (PRC2) is conserved from fungi to humans and represses gene transcription. However, the mechanism for recognition of methylated H3K27 remains unclear, especially in fungi. Here, we found that the bromo-adjacent homology (BAH)-plant homeodomain (PHD) domain containing protein BAH-PHD protein 1 (BP1) is a reader of H3K27 methylation in the cereal fungal pathogen Fusarium graminearum. BP1 interacts with the core PRC2 component Suz12 and directly binds methylated H3K27. BP1 is distributed in a subset of genomic regions marked by H3K27me3 and co-represses gene transcription. The BP1 deletion mutant shows identical phenotypes on mycelial growth and virulence, as well as similar expression profiles of secondary metabolite genes to the strain lacking the H3K27 methyltransferase Kmt6. More importantly, BP1 can directly bind DNA through its PHD finger, which might increase nucleosome residence and subsequently reinforce transcriptional repression in H3K27me3-marked target regions. A phylogenetic analysis showed that BP1 orthologs are mainly conserved in fungi. Overall, our findings provide novel insights into the mechanism by which PRC2 mediates gene repression in fungi, which is distinct from the PRC1-PRC2 system in plants and mammals.
Insights
In Fusarium graminearum, the protein BP1 reads histone H3 lysine 27 methylation (H3K27me3) to repress gene transcription. This fungal-specific mechanism differs from those in plants and mammals.
Area of Science:
- Molecular Biology
- Epigenetics
- Mycology
Background:
- Histone H3 lysine 27 methylation (H3K27me3) is a conserved epigenetic mark that represses gene transcription.
- The molecular mechanisms for recognizing H3K27me3 are not fully understood, particularly in fungal species.
Purpose of the Study:
- To identify and characterize H3K27me3 reader proteins in the fungal pathogen Fusarium graminearum.
- To elucidate the role of H3K27me3 recognition in gene regulation and fungal development.
Main Methods:
- Protein-protein interaction assays (e.g., co-immunoprecipitation) to identify BP1 interacting partners.
- Chromatin immunoprecipitation followed by sequencing (ChIP-seq) to determine genomic distribution of BP1 and H3K27me3.
- Phenotypic analysis of BP1 deletion mutants in terms of fungal growth, virulence, and secondary metabolite production.
- Phylogenetic analysis of BP1 orthologs across fungal species.
Main Results:
- Identified BAH-PHD protein 1 (BP1) as a direct H3K27me3 reader in Fusarium graminearum.
- BP1 interacts with the PRC2 component Suz12 and binds methylated H3K27 peptides.
- BP1 localizes to H3K27me3-marked regions and co-represses transcription.
- BP1 deletion mutants exhibit phenotypes similar to those lacking the H3K27 methyltransferase Kmt6.
- BP1's PHD finger binds DNA, potentially enhancing transcriptional repression.
Conclusions:
- BP1 is a key H3K27me3 reader in fungi, mediating transcriptional repression.
- The fungal H3K27me3 recognition mechanism involving BP1 is distinct from plant and mammalian systems.
- BP1 plays a significant role in regulating fungal gene expression, development, and virulence.
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