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Proteomic analysis of the carotenogenic yeast Xanthophyllomyces dendrorhous
BACKGROUND: The yeast Xanthophyllomyces dendrorhous is used for the microbiological production of the antioxidant carotenoid astaxanthin. In this study, we established an optimal protocol for protein extraction and performed the first proteomic analysis of the strain ATCC 24230. Protein profiles bef...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3224108/ https://www.ncbi.nlm.nih.gov/pubmed/21669001 http://dx.doi.org/10.1186/1471-2180-11-131 |
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author | Martinez-Moya, Pilar Watt, Steven Alexander Niehaus, Karsten Alcaíno, Jennifer Baeza, Marcelo Cifuentes, Víctor |
author_facet | Martinez-Moya, Pilar Watt, Steven Alexander Niehaus, Karsten Alcaíno, Jennifer Baeza, Marcelo Cifuentes, Víctor |
author_sort | Martinez-Moya, Pilar |
collection | PubMed |
description | BACKGROUND: The yeast Xanthophyllomyces dendrorhous is used for the microbiological production of the antioxidant carotenoid astaxanthin. In this study, we established an optimal protocol for protein extraction and performed the first proteomic analysis of the strain ATCC 24230. Protein profiles before and during the induction of carotenogenesis were determined by two-dimensional polyacrylamide gel electrophoresis and proteins were identified by mass spectrometry. RESULTS: Among the approximately 600 observed protein spots, 131 non-redundant proteins were identified. Proteomic analyses allowed us to identify 50 differentially expressed proteins that fall into several classes with distinct expression patterns. These analyses demonstrated that enzymes related to acetyl-CoA synthesis were more abundant prior to carotenogenesis. Later, redox- and stress-related proteins were up-regulated during the induction of carotenogenesis. For the carotenoid biosynthetic enzymes mevalonate kinase and phytoene/squalene synthase, we observed higher abundance during induction and/or accumulation of carotenoids. In addition, classical antioxidant enzymes, such as catalase, glutathione peroxidase and the cytosolic superoxide dismutases, were not identified. CONCLUSIONS: Our results provide an overview of potentially important carotenogenesis-related proteins, among which are proteins involved in carbohydrate and lipid biosynthetic pathways as well as several redox- and stress-related proteins. In addition, these results might indicate that X. dendrorhous accumulates astaxanthin under aerobic conditions to scavenge the reactive oxygen species (ROS) generated during metabolism. |
format | Online Article Text |
id | pubmed-3224108 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-32241082011-11-26 Proteomic analysis of the carotenogenic yeast Xanthophyllomyces dendrorhous Martinez-Moya, Pilar Watt, Steven Alexander Niehaus, Karsten Alcaíno, Jennifer Baeza, Marcelo Cifuentes, Víctor BMC Microbiol Research Article BACKGROUND: The yeast Xanthophyllomyces dendrorhous is used for the microbiological production of the antioxidant carotenoid astaxanthin. In this study, we established an optimal protocol for protein extraction and performed the first proteomic analysis of the strain ATCC 24230. Protein profiles before and during the induction of carotenogenesis were determined by two-dimensional polyacrylamide gel electrophoresis and proteins were identified by mass spectrometry. RESULTS: Among the approximately 600 observed protein spots, 131 non-redundant proteins were identified. Proteomic analyses allowed us to identify 50 differentially expressed proteins that fall into several classes with distinct expression patterns. These analyses demonstrated that enzymes related to acetyl-CoA synthesis were more abundant prior to carotenogenesis. Later, redox- and stress-related proteins were up-regulated during the induction of carotenogenesis. For the carotenoid biosynthetic enzymes mevalonate kinase and phytoene/squalene synthase, we observed higher abundance during induction and/or accumulation of carotenoids. In addition, classical antioxidant enzymes, such as catalase, glutathione peroxidase and the cytosolic superoxide dismutases, were not identified. CONCLUSIONS: Our results provide an overview of potentially important carotenogenesis-related proteins, among which are proteins involved in carbohydrate and lipid biosynthetic pathways as well as several redox- and stress-related proteins. In addition, these results might indicate that X. dendrorhous accumulates astaxanthin under aerobic conditions to scavenge the reactive oxygen species (ROS) generated during metabolism. BioMed Central 2011-06-13 /pmc/articles/PMC3224108/ /pubmed/21669001 http://dx.doi.org/10.1186/1471-2180-11-131 Text en Copyright ©2011 Martinez-Moya et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Martinez-Moya, Pilar Watt, Steven Alexander Niehaus, Karsten Alcaíno, Jennifer Baeza, Marcelo Cifuentes, Víctor Proteomic analysis of the carotenogenic yeast Xanthophyllomyces dendrorhous |
title | Proteomic analysis of the carotenogenic yeast Xanthophyllomyces dendrorhous |
title_full | Proteomic analysis of the carotenogenic yeast Xanthophyllomyces dendrorhous |
title_fullStr | Proteomic analysis of the carotenogenic yeast Xanthophyllomyces dendrorhous |
title_full_unstemmed | Proteomic analysis of the carotenogenic yeast Xanthophyllomyces dendrorhous |
title_short | Proteomic analysis of the carotenogenic yeast Xanthophyllomyces dendrorhous |
title_sort | proteomic analysis of the carotenogenic yeast xanthophyllomyces dendrorhous |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3224108/ https://www.ncbi.nlm.nih.gov/pubmed/21669001 http://dx.doi.org/10.1186/1471-2180-11-131 |
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