J Integr Plant Biol. ›› 2022, Vol. 64 ›› Issue (4): 901-914.DOI: 10.1111/jipb.13227

• Molecular Physiology • Previous Articles     Next Articles

The Arabidopsis NuA4 histone acetyltransferase complex is required for chlorophyll biosynthesis and photosynthesis

Jin‐Xing Zhou1,2†, Xiao‐Min Su1,2†, Si‐Yao Zheng2, Chan‐Juan Wu2, Yin‐Na Su2, Zhaodi Jiang2,3, Lin Li2, She Chen2,3 and Xin‐Jian He2,3*   

  1. 1. College of Life Sciences, Beijing Normal University, Beijing 100091, China
    2. National Institute of Biological Sciences, Beijing 102206, China
    3. Tsinghua Institute of Multidisciplinary Biomedical Research, Tsinghua University, Beijing 100084, China

    These authors contributed equally to this work.
    Correspondence: Xin‐Jian He (hexinjian@nibs.ac.cn)
  • Received:2021-11-14 Accepted:2022-01-14 Online:2022-01-19 Published:2022-04-01


Although two Enhancer of Polycomb-like proteins, EPL1A and EPL1B (EPL1A/B), are known to be conserved and characteristic subunits of the NuA4-type histone acetyltransferase complex in Arabidopsis thaliana, the biological function of EPL1A/B and the mechanism by which EPL1A/B function in the complex remain unknown. Here, we report that EPL1A/B are required for the histone acetyltransferase activity of the NuA4 complex on the nucleosomal histone H4 in vitro and for the enrichment of histone H4K5 acetylation at thousands of protein-coding genes in vivo. Our results suggest that EPL1A/B are required for linking the NuA4 catalytic subunits HISTONE ACETYLTRANSFERASE OF THE MYST FAMILY 1(HAM1) and HAM2 with accessory subunits in the NuA4 complex. EPL1A/B function redundantly in regulating plant development especially in chlorophyll biosynthesis and de-etiolation. The EPL1A/B-dependent transcription and H4K5Ac are enriched at genes involved in chlorophyll biosynthesis and photosynthesis. We also find that EAF6, another characteristic subunit of the NuA4 complex, contributes to de-etiolation. These results suggest that the Arabidopsis NuA4 complex components function as a whole to mediate histone acetylation and transcriptional activation specifically at light-responsive genes and are critical for photomorphogenesis.

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