Data from proteome analysis of Lasiodiplodia theobromae (Botryosphaeriaceae)

Trunk disease fungi are a global problem affecting many economically important fruiting trees. The Botryosphaeriaceae are a family of trunk disease fungi that require detailed biochemical characterization in order to gain insight into their pathogenicity. The application of a modified Folch extracti...

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Autores principales: Uranga, Carla C., Ghassemian, Majid, Hernández-Martínez, Rufina
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5447515/
https://www.ncbi.nlm.nih.gov/pubmed/28580409
http://dx.doi.org/10.1016/j.dib.2017.04.058
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author Uranga, Carla C.
Ghassemian, Majid
Hernández-Martínez, Rufina
author_facet Uranga, Carla C.
Ghassemian, Majid
Hernández-Martínez, Rufina
author_sort Uranga, Carla C.
collection PubMed
description Trunk disease fungi are a global problem affecting many economically important fruiting trees. The Botryosphaeriaceae are a family of trunk disease fungi that require detailed biochemical characterization in order to gain insight into their pathogenicity. The application of a modified Folch extraction to protein extraction from the Botryosphaeriaceae Lasiodiplodia theobromae generated an unprecedented data set of protein identifications from fragmentation analysis and de novo peptide sequencing of its proteome. This article contains data from protein identifications obtained from a database-dependent fragmentation analysis using three different proteomics algorithms (MSGF, Comet and X! Tandem via the SearchGUI proteomics pipeline program) and de novo peptide sequencing. Included are data sets of gene ontology annotations using an all-Uniprot ontology database, as well as a Saccharomyces cerevisiae-only and a Candida albicans-only ontology database, in order to discern between those proteins involved in common functions with S. cerevisiae and those in common with the pathogenic yeast C. albicans. Our results reveal the proteome of L. theobromae contains more ontological categories in common to C. albicans, yet possesses a much wider metabolic repertoire than any of the yeasts studied in this work. Many novel proteins of interest were identified for further biochemical characterization and annotation efforts, as further discussed in the article referencing this article (1). Interactive Cytoscape networks of molecular functions of identified peptides using an all-Uniprot ontological database are included. Data, including raw data, are available via ProteomeXchange with identifier PXD005283.
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spelling pubmed-54475152017-06-02 Data from proteome analysis of Lasiodiplodia theobromae (Botryosphaeriaceae) Uranga, Carla C. Ghassemian, Majid Hernández-Martínez, Rufina Data Brief Data Article Trunk disease fungi are a global problem affecting many economically important fruiting trees. The Botryosphaeriaceae are a family of trunk disease fungi that require detailed biochemical characterization in order to gain insight into their pathogenicity. The application of a modified Folch extraction to protein extraction from the Botryosphaeriaceae Lasiodiplodia theobromae generated an unprecedented data set of protein identifications from fragmentation analysis and de novo peptide sequencing of its proteome. This article contains data from protein identifications obtained from a database-dependent fragmentation analysis using three different proteomics algorithms (MSGF, Comet and X! Tandem via the SearchGUI proteomics pipeline program) and de novo peptide sequencing. Included are data sets of gene ontology annotations using an all-Uniprot ontology database, as well as a Saccharomyces cerevisiae-only and a Candida albicans-only ontology database, in order to discern between those proteins involved in common functions with S. cerevisiae and those in common with the pathogenic yeast C. albicans. Our results reveal the proteome of L. theobromae contains more ontological categories in common to C. albicans, yet possesses a much wider metabolic repertoire than any of the yeasts studied in this work. Many novel proteins of interest were identified for further biochemical characterization and annotation efforts, as further discussed in the article referencing this article (1). Interactive Cytoscape networks of molecular functions of identified peptides using an all-Uniprot ontological database are included. Data, including raw data, are available via ProteomeXchange with identifier PXD005283. Elsevier 2017-05-17 /pmc/articles/PMC5447515/ /pubmed/28580409 http://dx.doi.org/10.1016/j.dib.2017.04.058 Text en © 2017 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Data Article
Uranga, Carla C.
Ghassemian, Majid
Hernández-Martínez, Rufina
Data from proteome analysis of Lasiodiplodia theobromae (Botryosphaeriaceae)
title Data from proteome analysis of Lasiodiplodia theobromae (Botryosphaeriaceae)
title_full Data from proteome analysis of Lasiodiplodia theobromae (Botryosphaeriaceae)
title_fullStr Data from proteome analysis of Lasiodiplodia theobromae (Botryosphaeriaceae)
title_full_unstemmed Data from proteome analysis of Lasiodiplodia theobromae (Botryosphaeriaceae)
title_short Data from proteome analysis of Lasiodiplodia theobromae (Botryosphaeriaceae)
title_sort data from proteome analysis of lasiodiplodia theobromae (botryosphaeriaceae)
topic Data Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5447515/
https://www.ncbi.nlm.nih.gov/pubmed/28580409
http://dx.doi.org/10.1016/j.dib.2017.04.058
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