Cargando…
A Peroxisomal Long-Chain Acyl-CoA Synthetase from Glycine max Involved in Lipid Degradation
Seed storage oil, in the form of triacylglycerol (TAG), is degraded to provide carbon and energy during germination and early seedling growth by the fatty acid β-oxidation in the peroxisome. Although the pathways for lipid degradation have been uncovered, understanding of the exact involved enzymes...
Autores principales: | , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4081121/ https://www.ncbi.nlm.nih.gov/pubmed/24992019 http://dx.doi.org/10.1371/journal.pone.0100144 |
_version_ | 1782324070888505344 |
---|---|
author | Yu, Lili Tan, Xiaoli Jiang, Bingjun Sun, Xuegang Gu, Shoulai Han, Tianfu Hou, Wensheng |
author_facet | Yu, Lili Tan, Xiaoli Jiang, Bingjun Sun, Xuegang Gu, Shoulai Han, Tianfu Hou, Wensheng |
author_sort | Yu, Lili |
collection | PubMed |
description | Seed storage oil, in the form of triacylglycerol (TAG), is degraded to provide carbon and energy during germination and early seedling growth by the fatty acid β-oxidation in the peroxisome. Although the pathways for lipid degradation have been uncovered, understanding of the exact involved enzymes in soybean is still limited. Long-chain acyl-CoA synthetase (ACSL) is a critical enzyme that activates free fatty acid released from TAG to form the fatty acyl-CoA. Recent studies have shown the importance of ACSL in lipid degradation and synthesis, but few studies were focused on soybean. In this work, we cloned a ACSL gene from soybean and designated it as GmACSL2. Sequence analysis revealed that GmACSL2 encodes a protein of 733 amino acid residues, which is highly homologous to the ones in other higher plants. Complementation test showed that GmACSL2 could restore the growth of an ACS-deficient yeast strain (YB525). Co-expression assay in Nicotiana benthamiana indicated that GmACSL2 is located at peroxisome. Expression pattern analysis showed that GmACSL2 is highly expressed in germinating seedling and strongly induced 1 day after imbibition, which indicate that GmACSL2 may take part in the seed germination. GmACSL2 overexpression in yeast and soybean hairy root severely reduces the contents of the lipids and fatty acids, compared with controls in both cells, and enhances the β-oxidation efficiency in yeast. All these results suggest that GmACSL2 may take part in fatty acid and lipid degradation. In conclusion, peroxisomal GmACSL2 from Glycine max probably be involved in the lipid degradation during seed germination. |
format | Online Article Text |
id | pubmed-4081121 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-40811212014-07-10 A Peroxisomal Long-Chain Acyl-CoA Synthetase from Glycine max Involved in Lipid Degradation Yu, Lili Tan, Xiaoli Jiang, Bingjun Sun, Xuegang Gu, Shoulai Han, Tianfu Hou, Wensheng PLoS One Research Article Seed storage oil, in the form of triacylglycerol (TAG), is degraded to provide carbon and energy during germination and early seedling growth by the fatty acid β-oxidation in the peroxisome. Although the pathways for lipid degradation have been uncovered, understanding of the exact involved enzymes in soybean is still limited. Long-chain acyl-CoA synthetase (ACSL) is a critical enzyme that activates free fatty acid released from TAG to form the fatty acyl-CoA. Recent studies have shown the importance of ACSL in lipid degradation and synthesis, but few studies were focused on soybean. In this work, we cloned a ACSL gene from soybean and designated it as GmACSL2. Sequence analysis revealed that GmACSL2 encodes a protein of 733 amino acid residues, which is highly homologous to the ones in other higher plants. Complementation test showed that GmACSL2 could restore the growth of an ACS-deficient yeast strain (YB525). Co-expression assay in Nicotiana benthamiana indicated that GmACSL2 is located at peroxisome. Expression pattern analysis showed that GmACSL2 is highly expressed in germinating seedling and strongly induced 1 day after imbibition, which indicate that GmACSL2 may take part in the seed germination. GmACSL2 overexpression in yeast and soybean hairy root severely reduces the contents of the lipids and fatty acids, compared with controls in both cells, and enhances the β-oxidation efficiency in yeast. All these results suggest that GmACSL2 may take part in fatty acid and lipid degradation. In conclusion, peroxisomal GmACSL2 from Glycine max probably be involved in the lipid degradation during seed germination. Public Library of Science 2014-07-03 /pmc/articles/PMC4081121/ /pubmed/24992019 http://dx.doi.org/10.1371/journal.pone.0100144 Text en © 2014 Yu et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Yu, Lili Tan, Xiaoli Jiang, Bingjun Sun, Xuegang Gu, Shoulai Han, Tianfu Hou, Wensheng A Peroxisomal Long-Chain Acyl-CoA Synthetase from Glycine max Involved in Lipid Degradation |
title | A Peroxisomal Long-Chain Acyl-CoA Synthetase from Glycine max Involved in Lipid Degradation |
title_full | A Peroxisomal Long-Chain Acyl-CoA Synthetase from Glycine max Involved in Lipid Degradation |
title_fullStr | A Peroxisomal Long-Chain Acyl-CoA Synthetase from Glycine max Involved in Lipid Degradation |
title_full_unstemmed | A Peroxisomal Long-Chain Acyl-CoA Synthetase from Glycine max Involved in Lipid Degradation |
title_short | A Peroxisomal Long-Chain Acyl-CoA Synthetase from Glycine max Involved in Lipid Degradation |
title_sort | peroxisomal long-chain acyl-coa synthetase from glycine max involved in lipid degradation |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4081121/ https://www.ncbi.nlm.nih.gov/pubmed/24992019 http://dx.doi.org/10.1371/journal.pone.0100144 |
work_keys_str_mv | AT yulili aperoxisomallongchainacylcoasynthetasefromglycinemaxinvolvedinlipiddegradation AT tanxiaoli aperoxisomallongchainacylcoasynthetasefromglycinemaxinvolvedinlipiddegradation AT jiangbingjun aperoxisomallongchainacylcoasynthetasefromglycinemaxinvolvedinlipiddegradation AT sunxuegang aperoxisomallongchainacylcoasynthetasefromglycinemaxinvolvedinlipiddegradation AT gushoulai aperoxisomallongchainacylcoasynthetasefromglycinemaxinvolvedinlipiddegradation AT hantianfu aperoxisomallongchainacylcoasynthetasefromglycinemaxinvolvedinlipiddegradation AT houwensheng aperoxisomallongchainacylcoasynthetasefromglycinemaxinvolvedinlipiddegradation AT yulili peroxisomallongchainacylcoasynthetasefromglycinemaxinvolvedinlipiddegradation AT tanxiaoli peroxisomallongchainacylcoasynthetasefromglycinemaxinvolvedinlipiddegradation AT jiangbingjun peroxisomallongchainacylcoasynthetasefromglycinemaxinvolvedinlipiddegradation AT sunxuegang peroxisomallongchainacylcoasynthetasefromglycinemaxinvolvedinlipiddegradation AT gushoulai peroxisomallongchainacylcoasynthetasefromglycinemaxinvolvedinlipiddegradation AT hantianfu peroxisomallongchainacylcoasynthetasefromglycinemaxinvolvedinlipiddegradation AT houwensheng peroxisomallongchainacylcoasynthetasefromglycinemaxinvolvedinlipiddegradation |