Structural insight into the role of VAL1 B3 domain for targeting to FLC locus in Arabidopsis thaliana

Biochem Biophys Res Commun. 2018 Jun 22;501(2):415-422. doi: 10.1016/j.bbrc.2018.05.002. Epub 2018 May 10.

Abstract

Vernalization is a pivotal stage for some plants involving many epigenetic changes during cold exposure. In Arabidopsis, an essential step in vernalization for further flowering is successful silence the potent floral repressor Flowering Locus C (FLC) by repressing histone mark. AtVal1 is a multi-function protein containing five domains that participate into many recognition processes and is validated to recruit the repress histone modifier PHD-PRC2 complex and interact with components of the ASAP complex target to the FLC nucleation region through recognizing a cis element known as CME (cold memory element) by its plant-specific B3 domain. Here, we determine the crystal structure of the B3 domain in complex with Sph/RY motif in CME. Our structural analysis reveals the specific DNA recognition by B3 domain, combined with our in vitro experiments, we provide the structural insight into the important implication of AtVAL1-B3 domain in flowering process.

Keywords: B3 domain; DNA binding; FLC locus; Flowering; PRC2; Vernalization.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arabidopsis Proteins / chemistry*
  • Arabidopsis Proteins / genetics*
  • Arabidopsis Proteins / metabolism*
  • Crystallography, X-Ray
  • DNA, Plant / metabolism
  • MADS Domain Proteins / genetics*
  • MADS Domain Proteins / metabolism
  • Models, Molecular
  • Mutagenesis
  • Nucleotide Motifs
  • Protein Domains
  • Repressor Proteins / chemistry*
  • Repressor Proteins / genetics
  • Repressor Proteins / metabolism*

Substances

  • Arabidopsis Proteins
  • DNA, Plant
  • FLF protein, Arabidopsis
  • HSI2 protein, Arabidopsis
  • MADS Domain Proteins
  • Repressor Proteins