ELONGATED HYPOCOTYL 5 interacts with HISTONE DEACETYLASE 9 to suppress glucosinolate biosynthesis in Arabidopsis

Author:

Choi Dasom1ORCID,Kim Seong-Hyeon2ORCID,Choi Da-Min2ORCID,Moon Heewon1ORCID,Kim Jeong-Il2ORCID,Huq Enamul3ORCID,Kim Dong-Hwan1ORCID

Affiliation:

1. Department of Plant Science and Technology, Chung-Ang University , Anseong 17546 , Republic of Korea

2. Department of Integrative Food, Bioscience and Biotechnology, Chonnam National University , Gwangju 61186 , Republic of Korea

3. Department of Molecular Biosciences, University of Texas at Austin , Austin, TX 78712 , USA

Abstract

Abstract Glucosinolates (GSLs) are defensive secondary metabolites produced by Brassicaceae species in response to abiotic and biotic stresses. The biosynthesis of GSL compounds and the expression of GSL-related genes are highly modulated by endogenous signals (i.e. circadian clocks) and environmental cues, such as temperature, light, and pathogens. However, the detailed mechanism by which light signaling influences GSL metabolism remains poorly understood. In this study, we found that a light-signaling factor, ELONGATED HYPOCOTYL 5 (HY5), was involved in the regulation of GSL content under light conditions in Arabidopsis (Arabidopsis thaliana). In hy5-215 mutants, the transcript levels of GSL pathway genes were substantially upregulated compared with those in wild-type (WT) plants. The content of GSL compounds was also substantially increased in hy5-215 mutants, whereas 35S::HY5-GFP/hy5-215 transgenic lines exhibited comparable levels of GSL-related transcripts and GSL content to those in WT plants. HY5 physically interacts with HISTONE DEACETYLASE9 and binds to the proximal promoter region of MYB29 and IMD1 to suppress aliphatic GSL biosynthetic processes. These results demonstrate that HY5 suppresses GSL accumulation during the daytime, thus properly modulating GSL content daily in Arabidopsis plants.

Funder

National Research Foundation

Korean government

National Science Foundation

Publisher

Oxford University Press (OUP)

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