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Arabidopsis thaliana DGAT3 is a [2Fe-2S] protein involved in TAG biosynthesis
Acyl-CoA:diacylglycerol acyltransferases 3 (DGAT3) are described as plant cytosolic enzymes synthesizing triacylglycerol. Their protein sequences exhibit a thioredoxin-like ferredoxin domain typical of a class of ferredoxins harboring a [2Fe-2S] cluster. The Arabidopsis thaliana DGAT3 (AtDGAT3; At1g...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6250708/ https://www.ncbi.nlm.nih.gov/pubmed/30467384 http://dx.doi.org/10.1038/s41598-018-35545-7 |
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author | Aymé, Laure Arragain, Simon Canonge, Michel Baud, Sébastien Touati, Nadia Bimai, Ornella Jagic, Franjo Louis-Mondésir, Christelle Briozzo, Pierre Fontecave, Marc Chardot, Thierry |
author_facet | Aymé, Laure Arragain, Simon Canonge, Michel Baud, Sébastien Touati, Nadia Bimai, Ornella Jagic, Franjo Louis-Mondésir, Christelle Briozzo, Pierre Fontecave, Marc Chardot, Thierry |
author_sort | Aymé, Laure |
collection | PubMed |
description | Acyl-CoA:diacylglycerol acyltransferases 3 (DGAT3) are described as plant cytosolic enzymes synthesizing triacylglycerol. Their protein sequences exhibit a thioredoxin-like ferredoxin domain typical of a class of ferredoxins harboring a [2Fe-2S] cluster. The Arabidopsis thaliana DGAT3 (AtDGAT3; At1g48300) protein is detected in germinating seeds. The recombinant purified protein produced from Escherichia coli, although very unstable, exhibits DGAT activity in vitro. A shorter protein version devoid of its N-terminal putative chloroplast transit peptide, Δ46AtDGAT3, was more stable in vitro, allowing biochemical and spectroscopic characterization. The results obtained demonstrate the presence of a [2Fe-2S] cluster in the protein. To date, AtDGAT3 is the first metalloprotein described as a DGAT. |
format | Online Article Text |
id | pubmed-6250708 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-62507082018-11-29 Arabidopsis thaliana DGAT3 is a [2Fe-2S] protein involved in TAG biosynthesis Aymé, Laure Arragain, Simon Canonge, Michel Baud, Sébastien Touati, Nadia Bimai, Ornella Jagic, Franjo Louis-Mondésir, Christelle Briozzo, Pierre Fontecave, Marc Chardot, Thierry Sci Rep Article Acyl-CoA:diacylglycerol acyltransferases 3 (DGAT3) are described as plant cytosolic enzymes synthesizing triacylglycerol. Their protein sequences exhibit a thioredoxin-like ferredoxin domain typical of a class of ferredoxins harboring a [2Fe-2S] cluster. The Arabidopsis thaliana DGAT3 (AtDGAT3; At1g48300) protein is detected in germinating seeds. The recombinant purified protein produced from Escherichia coli, although very unstable, exhibits DGAT activity in vitro. A shorter protein version devoid of its N-terminal putative chloroplast transit peptide, Δ46AtDGAT3, was more stable in vitro, allowing biochemical and spectroscopic characterization. The results obtained demonstrate the presence of a [2Fe-2S] cluster in the protein. To date, AtDGAT3 is the first metalloprotein described as a DGAT. Nature Publishing Group UK 2018-11-22 /pmc/articles/PMC6250708/ /pubmed/30467384 http://dx.doi.org/10.1038/s41598-018-35545-7 Text en © The Author(s) 2018 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Aymé, Laure Arragain, Simon Canonge, Michel Baud, Sébastien Touati, Nadia Bimai, Ornella Jagic, Franjo Louis-Mondésir, Christelle Briozzo, Pierre Fontecave, Marc Chardot, Thierry Arabidopsis thaliana DGAT3 is a [2Fe-2S] protein involved in TAG biosynthesis |
title | Arabidopsis thaliana DGAT3 is a [2Fe-2S] protein involved in TAG biosynthesis |
title_full | Arabidopsis thaliana DGAT3 is a [2Fe-2S] protein involved in TAG biosynthesis |
title_fullStr | Arabidopsis thaliana DGAT3 is a [2Fe-2S] protein involved in TAG biosynthesis |
title_full_unstemmed | Arabidopsis thaliana DGAT3 is a [2Fe-2S] protein involved in TAG biosynthesis |
title_short | Arabidopsis thaliana DGAT3 is a [2Fe-2S] protein involved in TAG biosynthesis |
title_sort | arabidopsis thaliana dgat3 is a [2fe-2s] protein involved in tag biosynthesis |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6250708/ https://www.ncbi.nlm.nih.gov/pubmed/30467384 http://dx.doi.org/10.1038/s41598-018-35545-7 |
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