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

    Access Status
    Open access via publisher
    Authors
    Liu, Lifang
    Feizi, A.
    Österlund, T.
    Hjort, C.
    Nielsen, J.
    Date
    2014
    Type
    Journal Article
    
    Metadata
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    Citation
    Liu, L. and Feizi, A. and Österlund, T. and Hjort, C. and Nielsen, J. 2014. Genome-scale analysis of the high-efficient protein secretion system of Aspergillus oryzae. BMC Systems Biology. 8 (1): Article ID 73.
    Source Title
    BMC Systems Biology
    DOI
    10.1186/1752-0509-8-73
    School
    Centre for Crop Disease Management
    URI
    http://hdl.handle.net/20.500.11937/46581
    Collection
    • Curtin Research Publications
    Abstract

    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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