Histone H4R3 methylation catalyzed by SKB1/PRMT5 is required for maintaining shoot apical meristem

PLoS One. 2013 Dec 12;8(12):e83258. doi: 10.1371/journal.pone.0083258. eCollection 2013.

Abstract

The shoot apical meristem (SAM) is the source of all of the above-ground tissues and organs in post-embryonic development in higher plants. Studies have proven that the expression of genes constituting the WUSCHEL (WUS)-CLAVATA (CLV) feedback loop is critical for the SAM maintenance. Several histone lysine acetylation and methylation markers have been proven to regulate the transcription level of WUS. However, little is known about how histone arginine methylation regulates the expression of WUS and other genes. Here, we report that H4R3 symmetric dimethylation (H4R3sme2) mediated by SKB1/PRMT5 represses the expression of CORYNE (CRN) to maintain normal SAM geometrics. SKB1 lesion results in small SAM size in Arabidopsis, as well as down-regulated expression of WUS and CLV3. Up-regulation of WUS expression enlarges SAM size in skb1 mutant plants. We find that SKB1 and H4R3sme2 associate with the chromatin of the CRN locus to down-regulate its transcription. Mutation of CRN rescues the expression of WUS and the small SAM size of skb1. Thus, SKB1 and SKB1-mediated H4R3sme2 are required for the maintenance of SAM in Arabidopsis seedlings.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arabidopsis / genetics
  • Arabidopsis / metabolism*
  • Arabidopsis Proteins / genetics
  • Arabidopsis Proteins / metabolism*
  • Gene Expression Regulation, Enzymologic / physiology
  • Gene Expression Regulation, Plant / physiology
  • Histones / genetics
  • Histones / metabolism*
  • Meristem / cytology
  • Meristem / metabolism*
  • Methylation
  • Protein Serine-Threonine Kinases / biosynthesis
  • Protein-Arginine N-Methyltransferases / genetics
  • Protein-Arginine N-Methyltransferases / metabolism*
  • Receptors, Cell Surface / biosynthesis
  • Seedlings / genetics
  • Seedlings / metabolism*

Substances

  • Arabidopsis Proteins
  • Histones
  • Receptors, Cell Surface
  • PRMT5 protein, Arabidopsis
  • Protein-Arginine N-Methyltransferases
  • CORYNE protein, Arabidopsis
  • Protein Serine-Threonine Kinases

Grants and funding

This research was supported by the National Basic Research Program of China, grant 2007CB948202 (to Shilai Bao), and the Chinese National Natural and Sciences Foundation, grants 31071120, 91019018 (to Shilai Bao), and 31071121 (to Yan Zhao). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.