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Subcellular Localizations of Catalase and Exogenously Added Fatty Acid in Chlamydomonas reinhardtii
Fatty acids are important biological components, yet the metabolism of fatty acids in microalgae is not clearly understood. Previous studies found that Chlamydomonas reinhardtii, the model microalga, incorporates exogenously added fatty acids but metabolizes them differently from animals and yeast....
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8391285/ https://www.ncbi.nlm.nih.gov/pubmed/34440712 http://dx.doi.org/10.3390/cells10081940 |
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author | Kato, Naohiro Nelson, Gabela Lauersen, Kyle J. |
author_facet | Kato, Naohiro Nelson, Gabela Lauersen, Kyle J. |
author_sort | Kato, Naohiro |
collection | PubMed |
description | Fatty acids are important biological components, yet the metabolism of fatty acids in microalgae is not clearly understood. Previous studies found that Chlamydomonas reinhardtii, the model microalga, incorporates exogenously added fatty acids but metabolizes them differently from animals and yeast. Furthermore, a recent metabolic flux analysis found that the majority of lipid turnover in C. reinhardtii is the recycling of acyl chains from and to membranes, rather than β -oxidation. This indicates that for the alga, the maintenance of existing acyl chains may be more valuable than their breakdown for energy. To gain cell-biological knowledge of fatty acid metabolism in C. reinhardtii, we conducted microscopy analysis with fluorescent probes. First, we found that CAT1 (catalase isoform 1) is in the peroxisomes while CAT2 (catalase isoform 2) is localized in the endoplasmic reticulum, indicating the alga is capable of detoxifying hydrogen peroxide that would be produced during β-oxidation in the peroxisomes. Second, we compared the localization of exogenously added FL-C16 (fluorescently labelled palmitic acid) with fluorescently marked endosomes, mitochondria, peroxisomes, lysosomes, and lipid droplets. We found that exogenously added FL-C16 are incorporated and compartmentalized via a non-endocytic route within 10 min. However, the fluorescence signals from FL-C16 did not colocalize with any marked organelles, including peroxisomes. During triacylglycerol accumulation, the fluorescence signals from FL-C16 were localized in lipid droplets. These results support the idea that membrane turnover is favored over β-oxidation in C. reinhardtii. The knowledge gained in these analyses would aid further studies of the fatty acid metabolism. |
format | Online Article Text |
id | pubmed-8391285 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-83912852021-08-28 Subcellular Localizations of Catalase and Exogenously Added Fatty Acid in Chlamydomonas reinhardtii Kato, Naohiro Nelson, Gabela Lauersen, Kyle J. Cells Article Fatty acids are important biological components, yet the metabolism of fatty acids in microalgae is not clearly understood. Previous studies found that Chlamydomonas reinhardtii, the model microalga, incorporates exogenously added fatty acids but metabolizes them differently from animals and yeast. Furthermore, a recent metabolic flux analysis found that the majority of lipid turnover in C. reinhardtii is the recycling of acyl chains from and to membranes, rather than β -oxidation. This indicates that for the alga, the maintenance of existing acyl chains may be more valuable than their breakdown for energy. To gain cell-biological knowledge of fatty acid metabolism in C. reinhardtii, we conducted microscopy analysis with fluorescent probes. First, we found that CAT1 (catalase isoform 1) is in the peroxisomes while CAT2 (catalase isoform 2) is localized in the endoplasmic reticulum, indicating the alga is capable of detoxifying hydrogen peroxide that would be produced during β-oxidation in the peroxisomes. Second, we compared the localization of exogenously added FL-C16 (fluorescently labelled palmitic acid) with fluorescently marked endosomes, mitochondria, peroxisomes, lysosomes, and lipid droplets. We found that exogenously added FL-C16 are incorporated and compartmentalized via a non-endocytic route within 10 min. However, the fluorescence signals from FL-C16 did not colocalize with any marked organelles, including peroxisomes. During triacylglycerol accumulation, the fluorescence signals from FL-C16 were localized in lipid droplets. These results support the idea that membrane turnover is favored over β-oxidation in C. reinhardtii. The knowledge gained in these analyses would aid further studies of the fatty acid metabolism. MDPI 2021-07-30 /pmc/articles/PMC8391285/ /pubmed/34440712 http://dx.doi.org/10.3390/cells10081940 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Kato, Naohiro Nelson, Gabela Lauersen, Kyle J. Subcellular Localizations of Catalase and Exogenously Added Fatty Acid in Chlamydomonas reinhardtii |
title | Subcellular Localizations of Catalase and Exogenously Added Fatty Acid in Chlamydomonas reinhardtii |
title_full | Subcellular Localizations of Catalase and Exogenously Added Fatty Acid in Chlamydomonas reinhardtii |
title_fullStr | Subcellular Localizations of Catalase and Exogenously Added Fatty Acid in Chlamydomonas reinhardtii |
title_full_unstemmed | Subcellular Localizations of Catalase and Exogenously Added Fatty Acid in Chlamydomonas reinhardtii |
title_short | Subcellular Localizations of Catalase and Exogenously Added Fatty Acid in Chlamydomonas reinhardtii |
title_sort | subcellular localizations of catalase and exogenously added fatty acid in chlamydomonas reinhardtii |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8391285/ https://www.ncbi.nlm.nih.gov/pubmed/34440712 http://dx.doi.org/10.3390/cells10081940 |
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