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

Baixing Wu; Mengmeng Zhang; Shichen Su; Hehua Liu; Jianhua Gan; Jinbiao Ma

doi:10.1016/j.bbrc.2018.05.002

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.

Authors

Baixing Wu¹, Mengmeng Zhang², Shichen Su², Hehua Liu³, Jianhua Gan³, Jinbiao Ma⁴

Affiliations

¹ State Key Laboratory of Genetic Engineering, Collaborative Innovation Centre of Genetics and Development, Department of Biochemistry, Institute of Plant Biology, School of Life Sciences, Fudan University, Shanghai 200438, China. Electronic address: bxwu15@fudan.edu.cn.
² State Key Laboratory of Genetic Engineering, Collaborative Innovation Centre of Genetics and Development, Department of Biochemistry, Institute of Plant Biology, School of Life Sciences, Fudan University, Shanghai 200438, China.
³ State Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, Department of Physiology and Biophysics, School of Life Sciences, Fudan University, Shanghai, 200438, China.
⁴ State Key Laboratory of Genetic Engineering, Collaborative Innovation Centre of Genetics and Development, Department of Biochemistry, Institute of Plant Biology, School of Life Sciences, Fudan University, Shanghai 200438, China. Electronic address: majb@fudan.edu.cn.

PMID: 29733847
DOI: 10.1016/j.bbrc.2018.05.002

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