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Comprehensive subcellular topologies of polypeptides in Streptomyces

BACKGROUND: Members of the genus Streptomyces are Gram-positive bacteria that are used as important cell factories to produce secondary metabolites and secrete heterologous proteins. They possess some of the largest bacterial genomes and thus proteomes. Understanding their complex proteomes and meta...

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Autores principales: Tsolis, Konstantinos C., Tsare, Evridiki-Pandora, Orfanoudaki, Georgia, Busche, Tobias, Kanaki, Katerina, Ramakrishnan, Reshmi, Rousseau, Frederic, Schymkowitz, Joost, Rückert, Christian, Kalinowski, Jörn, Anné, Jozef, Karamanou, Spyridoula, Klapa, Maria I., Economou, Anastassios
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5853079/
https://www.ncbi.nlm.nih.gov/pubmed/29544487
http://dx.doi.org/10.1186/s12934-018-0892-0
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author Tsolis, Konstantinos C.
Tsare, Evridiki-Pandora
Orfanoudaki, Georgia
Busche, Tobias
Kanaki, Katerina
Ramakrishnan, Reshmi
Rousseau, Frederic
Schymkowitz, Joost
Rückert, Christian
Kalinowski, Jörn
Anné, Jozef
Karamanou, Spyridoula
Klapa, Maria I.
Economou, Anastassios
author_facet Tsolis, Konstantinos C.
Tsare, Evridiki-Pandora
Orfanoudaki, Georgia
Busche, Tobias
Kanaki, Katerina
Ramakrishnan, Reshmi
Rousseau, Frederic
Schymkowitz, Joost
Rückert, Christian
Kalinowski, Jörn
Anné, Jozef
Karamanou, Spyridoula
Klapa, Maria I.
Economou, Anastassios
author_sort Tsolis, Konstantinos C.
collection PubMed
description BACKGROUND: Members of the genus Streptomyces are Gram-positive bacteria that are used as important cell factories to produce secondary metabolites and secrete heterologous proteins. They possess some of the largest bacterial genomes and thus proteomes. Understanding their complex proteomes and metabolic regulation will improve any genetic engineering approach. RESULTS: Here, we performed a comprehensive annotation of the subcellular localization of the proteome of Streptomyces lividans TK24 and developed the Subcellular Topology of Polypeptides in Streptomyces database (SToPSdb) to make this information widely accessible. We first introduced a uniform, improved nomenclature that re-annotated the names of ~ 4000 proteins based on functional and structural information. Then protein localization was assigned de novo using prediction tools and edited by manual curation for 7494 proteins, including information for 183 proteins that resulted from a recent genome re-annotation and are not available in current databases. The S. lividans proteome was also linked with those of other model bacterial strains including Streptomyces coelicolor A3(2) and Escherichia coli K-12, based on protein homology, and can be accessed through an open web interface. Finally, experimental data derived from proteomics experiments have been incorporated and provide validation for protein existence or topology for 579 proteins. Proteomics also reveals proteins released from vesicles that bleb off the membrane. All export systems known in S. lividans are also presented and exported proteins assigned export routes, where known. CONCLUSIONS: SToPSdb provides an updated and comprehensive protein localization annotation resource for S. lividans and other streptomycetes. It forms the basis for future linking to databases containing experimental data of proteomics, genomics and metabolomics studies for this organism. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12934-018-0892-0) contains supplementary material, which is available to authorized users.
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spelling pubmed-58530792018-03-22 Comprehensive subcellular topologies of polypeptides in Streptomyces Tsolis, Konstantinos C. Tsare, Evridiki-Pandora Orfanoudaki, Georgia Busche, Tobias Kanaki, Katerina Ramakrishnan, Reshmi Rousseau, Frederic Schymkowitz, Joost Rückert, Christian Kalinowski, Jörn Anné, Jozef Karamanou, Spyridoula Klapa, Maria I. Economou, Anastassios Microb Cell Fact Research BACKGROUND: Members of the genus Streptomyces are Gram-positive bacteria that are used as important cell factories to produce secondary metabolites and secrete heterologous proteins. They possess some of the largest bacterial genomes and thus proteomes. Understanding their complex proteomes and metabolic regulation will improve any genetic engineering approach. RESULTS: Here, we performed a comprehensive annotation of the subcellular localization of the proteome of Streptomyces lividans TK24 and developed the Subcellular Topology of Polypeptides in Streptomyces database (SToPSdb) to make this information widely accessible. We first introduced a uniform, improved nomenclature that re-annotated the names of ~ 4000 proteins based on functional and structural information. Then protein localization was assigned de novo using prediction tools and edited by manual curation for 7494 proteins, including information for 183 proteins that resulted from a recent genome re-annotation and are not available in current databases. The S. lividans proteome was also linked with those of other model bacterial strains including Streptomyces coelicolor A3(2) and Escherichia coli K-12, based on protein homology, and can be accessed through an open web interface. Finally, experimental data derived from proteomics experiments have been incorporated and provide validation for protein existence or topology for 579 proteins. Proteomics also reveals proteins released from vesicles that bleb off the membrane. All export systems known in S. lividans are also presented and exported proteins assigned export routes, where known. CONCLUSIONS: SToPSdb provides an updated and comprehensive protein localization annotation resource for S. lividans and other streptomycetes. It forms the basis for future linking to databases containing experimental data of proteomics, genomics and metabolomics studies for this organism. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12934-018-0892-0) contains supplementary material, which is available to authorized users. BioMed Central 2018-03-15 /pmc/articles/PMC5853079/ /pubmed/29544487 http://dx.doi.org/10.1186/s12934-018-0892-0 Text en © The Author(s) 2018 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. 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
Tsolis, Konstantinos C.
Tsare, Evridiki-Pandora
Orfanoudaki, Georgia
Busche, Tobias
Kanaki, Katerina
Ramakrishnan, Reshmi
Rousseau, Frederic
Schymkowitz, Joost
Rückert, Christian
Kalinowski, Jörn
Anné, Jozef
Karamanou, Spyridoula
Klapa, Maria I.
Economou, Anastassios
Comprehensive subcellular topologies of polypeptides in Streptomyces
title Comprehensive subcellular topologies of polypeptides in Streptomyces
title_full Comprehensive subcellular topologies of polypeptides in Streptomyces
title_fullStr Comprehensive subcellular topologies of polypeptides in Streptomyces
title_full_unstemmed Comprehensive subcellular topologies of polypeptides in Streptomyces
title_short Comprehensive subcellular topologies of polypeptides in Streptomyces
title_sort comprehensive subcellular topologies of polypeptides in streptomyces
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5853079/
https://www.ncbi.nlm.nih.gov/pubmed/29544487
http://dx.doi.org/10.1186/s12934-018-0892-0
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