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Variation in sulfur and selenium accumulation is controlled by naturally occurring isoforms of the key sulfur assimilation enzyme ADENOSINE 5'-PHOSPHOSULFATE REDUCTASE2 across the Arabidopsis species range
DY. Chao, P. Baraniecka, J. Danku, A. Koprivova, B. Lahner, H. Luo, E. Yakubova, B. Dilkes, S. Kopriva, DE. Salt,
Language English Country United States
Document type Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't
Grant support
R01 GM078536
NIGMS NIH HHS - United States
2R01GM078536
NIGMS NIH HHS - United States
BB/J004561/1
Biotechnology and Biological Sciences Research Council - United Kingdom
BB/L000113/1
Biotechnology and Biological Sciences Research Council - United Kingdom
NLK
Free Medical Journals
from 1926 to 1 year ago
Open Access Digital Library
from 1926-01-01
PubMed
25245030
DOI
10.1104/pp.114.247825
Knihovny.cz E-resources
- MeSH
- Arabidopsis genetics metabolism MeSH
- Genome-Wide Association Study MeSH
- Phenotype MeSH
- Gene Frequency MeSH
- Genetic Variation MeSH
- Plants, Genetically Modified MeSH
- Isoenzymes genetics metabolism MeSH
- Plant Leaves metabolism MeSH
- Oxidoreductases Acting on Sulfur Group Donors genetics metabolism MeSH
- Arabidopsis Proteins genetics metabolism MeSH
- Selenium metabolism MeSH
- Sulfur metabolism MeSH
- Sulfates metabolism MeSH
- Amino Acid Substitution MeSH
- Plant Shoots metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Research Support, N.I.H., Extramural MeSH
- Geographicals
- Czech Republic MeSH
- Sweden MeSH
Natural variation allows the investigation of both the fundamental functions of genes and their role in local adaptation. As one of the essential macronutrients, sulfur is vital for plant growth and development and also for crop yield and quality. Selenium and sulfur are assimilated by the same process, and although plants do not require selenium, plant-based selenium is an important source of this essential element for animals. Here, we report the use of linkage mapping in synthetic F2 populations and complementation to investigate the genetic architecture of variation in total leaf sulfur and selenium concentrations in a diverse set of Arabidopsis (Arabidopsis thaliana) accessions. We identify in accessions collected from Sweden and the Czech Republic two variants of the enzyme ADENOSINE 5'-PHOSPHOSULFATE REDUCTASE2 (APR2) with strongly diminished catalytic capacity. APR2 is a key enzyme in both sulfate and selenate reduction, and its reduced activity in the loss-of-function allele apr2-1 and the two Arabidopsis accessions Hodonín and Shahdara leads to a lowering of sulfur flux from sulfate into the reduced sulfur compounds, cysteine and glutathione, and into proteins, concomitant with an increase in the accumulation of sulfate in leaves. We conclude from our observation, and the previously identified weak allele of APR2 from the Shahdara accession collected in Tadjikistan, that the catalytic capacity of APR2 varies by 4 orders of magnitude across the Arabidopsis species range, driving significant differences in sulfur and selenium metabolism. The selective benefit, if any, of this large variation remains to be explored.
Department of Horticulture and Landscape Architecture Purdue University West Lafayette Indiana 47907
Department of Metabolic Biology John Innes Centre Norwich NR4 7UH United Kingdom
References provided by Crossref.org
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- $a Chao, Dai-Yin $u Institute of Biological and Environmental Sciences, University of Aberdeen, Aberdeen AB24 3UU, United Kingdom (D.-Y.C., J.D., D.E.S.);Department of Metabolic Biology, John Innes Centre, Norwich NR4 7UH, United Kingdom (P.B., A.K., S.K.); andDepartment of Horticulture and Landscape Architecture, Purdue University, West Lafayette, Indiana 47907 (B.L., H.L., E.Y., B.D.).
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