Nuclear Localised MORE SULPHUR ACCUMULATION1 Epigenetically Regulates Sulphur Homeostasis in Arabidopsis thaliana

Autor: Hermann Bauwe, Brian P. Dilkes, Dai-Yin Chao, Francisco J. Sandoval, Markus Wirtz, David E. Salt, Stanislav Kopriva, Sanja Roje, Xin-Yuan Huang, Steffen Müller, John Danku, Anna Koprivova, Rüdiger Hell
Jazyk: angličtina
Rok vydání: 2016
Předmět:
0106 biological sciences
0301 basic medicine
Cancer Research
Leaves
S-Adenosylmethionine
Agricultural Biotechnology
Mutant
Arabidopsis
Artificial Gene Amplification and Extension
Plant Science
01 natural sciences
Biochemistry
Genetically Modified Plants
Polymerase Chain Reaction
Epigenesis
Genetic

chemistry.chemical_compound
Gene expression
Homeostasis
Genetics (clinical)
2. Zero hunger
DNA methylation
Sulfates
Plant Anatomy
Genetically Modified Organisms
Nuclear Proteins
Agriculture
Methylation
Plants
Glutathione
Chromatin
Nucleic acids
Chemistry
medicine.anatomical_structure
Physical Sciences
Epigenetics
DNA modification
Genetic Engineering
Chromatin modification
Research Article
Chromosome biology
Chemical Elements
Biotechnology
Cell biology
lcsh:QH426-470
Arabidopsis Thaliana
Anion Transport Proteins
Active Transport
Cell Nucleus

Brassica
Biology
Research and Analysis Methods
03 medical and health sciences
Model Organisms
Biosynthesis
Plant and Algal Models
medicine
Genetics
Molecular Biology Techniques
Gene
Molecular Biology
Ecology
Evolution
Behavior and Systematics

Cell Nucleus
Biology and life sciences
Arabidopsis Proteins
Chemical Compounds
Organisms
DNA
lcsh:Genetics
Cell nucleus
030104 developmental biology
chemistry
13. Climate action
Salts
Plant Biotechnology
Sulfur
010606 plant biology & botany
Zdroj: PLoS Genetics
PLoS Genetics, Vol 12, Iss 9, p e1006298 (2016)
ISSN: 1553-7404
1553-7390
Popis: Sulphur (S) is an essential element for all living organisms. The uptake, assimilation and metabolism of S in plants are well studied. However, the regulation of S homeostasis remains largely unknown. Here, we report on the identification and characterisation of the more sulphur accumulation1 (msa1-1) mutant. The MSA1 protein is localized to the nucleus and is required for both S-adenosylmethionine (SAM) production and DNA methylation. Loss of function of the nuclear localised MSA1 leads to a reduction in SAM in roots and a strong S-deficiency response even at ample S supply, causing an over-accumulation of sulphate, sulphite, cysteine and glutathione. Supplementation with SAM suppresses this high S phenotype. Furthermore, mutation of MSA1 affects genome-wide DNA methylation, including the methylation of S-deficiency responsive genes. Elevated S accumulation in msa1-1 requires the increased expression of the sulphate transporter genes SULTR1;1 and SULTR1;2 which are also differentially methylated in msa1-1. Our results suggest a novel function for MSA1 in the nucleus in regulating SAM biosynthesis and maintaining S homeostasis epigenetically via DNA methylation.
Author Summary Sulphur is an essential element for all living organisms including plants. Plants take up sulphur from the soil mainly in the form of inorganic sulphate. The uptake of sulphate and assimilation of sulphur have been well studied. However, the regulation of sulphur accumulation in plants remains largely unknown. In this study, we characterize the high leaf sulphur mutant more sulphur accumulation1 (msa1-1) and demonstrate the function of MSA1 in controlling sulphur accumulation in Arabidopsis thaliana. The MSA1 protein is localized to the nucleus and is required for the biosynthesis of S-adenosylmethionine (SAM) which is a universal methyl donor for many methylation reactions, including DNA methylation. Loss of function of MSA1 reduces the SAM level in roots and affects genome-wide DNA methylation, including the methylation of sulphate transporter genes. We show that the high sulphur phenotype of msa1-1 requires elevated expression of the sulphate transporter genes which are differentially methylated in msa1-1. Our results suggest a connection between sulphur homeostasis and DNA methylation that is mediated by MSA1.
Databáze: OpenAIRE