Abstract

The different genome-wide distributions of tri-methylation at H3K36 (H3K36me3) in various species suggest diverse mechanisms for H3K36me3 establishment during evolution. Here, we show that the transcription factor OsSUF4 recognizes a specific 7-bp DNA element, broadly distributes throughout the rice genome, and recruits the H3K36 methyltransferase SDG725 to target a set of genes including the key florigen genes RFT1 and Hd3a to promote flowering in rice. Biochemical and structural analyses indicate that several positive residues within the zinc finger domain are vital for OsSUF4 function in planta. Our results reveal a regulatory mechanism contributing to H3K36me3 distribution in plants.

Highlights

  • The different genome-wide distributions of tri-methylation at H3K36 (H3K36me3) in various species suggest diverse mechanisms for H3K36me[3] establishment during evolution

  • The distribution of H3K36 in D. melanogaster, mice, and humans was mainly enriched at the 3′ end of the gene body, with an apparent peak close to the transcription terminal site (TTS)

  • These results proved that the transcription factor OsSUF4 physically interacts with the H3K36-specific methyltransferase SDG725 in rice

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Summary

Introduction

The different genome-wide distributions of tri-methylation at H3K36 (H3K36me3) in various species suggest diverse mechanisms for H3K36me[3] establishment during evolution. We show that the transcription factor OsSUF4 recognizes a specific 7-bp DNA element, broadly distributes throughout the rice genome, and recruits the H3K36 methyltransferase SDG725 to target a set of genes including the key florigen genes RFT1 and Hd3a to promote flowering in rice. H3K36me[3] is mainly distributed at the 3′ end of the gene body[7], but it is close to the transcription start site (TSS) in plants[8,9] It suggests that different mechanisms for H3K36me[3] establishment and function may exist between plants and animals. Arabidopsis SDG8 and rice SDG725 are the closest homologs of yeast SET2 and human SETD2, and they share similar domain organization This evolutionary conservation in modifying enzymes seems to conflict with the divergence in genomic distributions of H3K36me[3], which prompted us to study the mechanisms underlying the establishment of H3K36 methylation in various species. Our findings highlight that distinct binding proteins of histone-modifying enzymes may lead to divergence in histone methylation distribution and eventually exhibit individual functions in various species

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