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Genome-scale analysis of the high-efficient protein secretion system of Aspergillus oryzae

BACKGROUND: The koji mold, Aspergillus oryzae is widely used for the production of industrial enzymes due to its particularly high protein secretion capacity and ability to perform post-translational modifications. However, systemic analysis of its secretion system is lacking, generally due to the p...

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Autores principales: Liu, Lifang, Feizi, Amir, Österlund, Tobias, Hjort, Carsten, Nielsen, Jens
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4086290/
https://www.ncbi.nlm.nih.gov/pubmed/24961398
http://dx.doi.org/10.1186/1752-0509-8-73
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author Liu, Lifang
Feizi, Amir
Österlund, Tobias
Hjort, Carsten
Nielsen, Jens
author_facet Liu, Lifang
Feizi, Amir
Österlund, Tobias
Hjort, Carsten
Nielsen, Jens
author_sort Liu, Lifang
collection PubMed
description BACKGROUND: The koji mold, Aspergillus oryzae is widely used for the production of industrial enzymes due to its particularly high protein secretion capacity and ability to perform post-translational modifications. However, systemic analysis of its secretion system is lacking, generally due to the poorly annotated proteome. RESULTS: Here we defined a functional protein secretory component list of A. oryzae using a previously reported secretory model of S. cerevisiae as scaffold. Additional secretory components were obtained by blast search with the functional components reported in other closely related fungal species such as Aspergillus nidulans and Aspergillus niger. To evaluate the defined component list, we performed transcriptome analysis on three α-amylase over-producing strains with varying levels of secretion capacities. Specifically, secretory components involved in the ER-associated processes (including components involved in the regulation of transport between ER and Golgi) were significantly up-regulated, with many of them never been identified for A. oryzae before. Furthermore, we defined a complete list of the putative A. oryzae secretome and monitored how it was affected by overproducing amylase. CONCLUSION: In combination with the transcriptome data, the most complete secretory component list and the putative secretome, we improved the systemic understanding of the secretory machinery of A. oryzae in response to high levels of protein secretion. The roles of many newly predicted secretory components were experimentally validated and the enriched component list provides a better platform for driving more mechanistic studies of the protein secretory pathway in this industrially important fungus.
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spelling pubmed-40862902014-07-09 Genome-scale analysis of the high-efficient protein secretion system of Aspergillus oryzae Liu, Lifang Feizi, Amir Österlund, Tobias Hjort, Carsten Nielsen, Jens BMC Syst Biol Research Article BACKGROUND: The koji mold, Aspergillus oryzae is widely used for the production of industrial enzymes due to its particularly high protein secretion capacity and ability to perform post-translational modifications. However, systemic analysis of its secretion system is lacking, generally due to the poorly annotated proteome. RESULTS: Here we defined a functional protein secretory component list of A. oryzae using a previously reported secretory model of S. cerevisiae as scaffold. Additional secretory components were obtained by blast search with the functional components reported in other closely related fungal species such as Aspergillus nidulans and Aspergillus niger. To evaluate the defined component list, we performed transcriptome analysis on three α-amylase over-producing strains with varying levels of secretion capacities. Specifically, secretory components involved in the ER-associated processes (including components involved in the regulation of transport between ER and Golgi) were significantly up-regulated, with many of them never been identified for A. oryzae before. Furthermore, we defined a complete list of the putative A. oryzae secretome and monitored how it was affected by overproducing amylase. CONCLUSION: In combination with the transcriptome data, the most complete secretory component list and the putative secretome, we improved the systemic understanding of the secretory machinery of A. oryzae in response to high levels of protein secretion. The roles of many newly predicted secretory components were experimentally validated and the enriched component list provides a better platform for driving more mechanistic studies of the protein secretory pathway in this industrially important fungus. BioMed Central 2014-06-24 /pmc/articles/PMC4086290/ /pubmed/24961398 http://dx.doi.org/10.1186/1752-0509-8-73 Text en Copyright © 2014 Liu et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/4.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Research Article
Liu, Lifang
Feizi, Amir
Österlund, Tobias
Hjort, Carsten
Nielsen, Jens
Genome-scale analysis of the high-efficient protein secretion system of Aspergillus oryzae
title Genome-scale analysis of the high-efficient protein secretion system of Aspergillus oryzae
title_full Genome-scale analysis of the high-efficient protein secretion system of Aspergillus oryzae
title_fullStr Genome-scale analysis of the high-efficient protein secretion system of Aspergillus oryzae
title_full_unstemmed Genome-scale analysis of the high-efficient protein secretion system of Aspergillus oryzae
title_short Genome-scale analysis of the high-efficient protein secretion system of Aspergillus oryzae
title_sort genome-scale analysis of the high-efficient protein secretion system of aspergillus oryzae
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4086290/
https://www.ncbi.nlm.nih.gov/pubmed/24961398
http://dx.doi.org/10.1186/1752-0509-8-73
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