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A Protein Complex Map of Trypanosoma brucei
The functions of the majority of trypanosomatid-specific proteins are unknown, hindering our understanding of the biology and pathogenesis of Trypanosomatida. While protein-protein interactions are highly informative about protein function, a global map of protein interactions and complexes is still...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4798371/ https://www.ncbi.nlm.nih.gov/pubmed/26991453 http://dx.doi.org/10.1371/journal.pntd.0004533 |
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author | Gazestani, Vahid H. Nikpour, Najmeh Mehta, Vaibhav Najafabadi, Hamed S. Moshiri, Houtan Jardim, Armando Salavati, Reza |
author_facet | Gazestani, Vahid H. Nikpour, Najmeh Mehta, Vaibhav Najafabadi, Hamed S. Moshiri, Houtan Jardim, Armando Salavati, Reza |
author_sort | Gazestani, Vahid H. |
collection | PubMed |
description | The functions of the majority of trypanosomatid-specific proteins are unknown, hindering our understanding of the biology and pathogenesis of Trypanosomatida. While protein-protein interactions are highly informative about protein function, a global map of protein interactions and complexes is still lacking for these important human parasites. Here, benefiting from in-depth biochemical fractionation, we systematically interrogated the co-complex interactions of more than 3354 protein groups in procyclic life stage of Trypanosoma brucei, the protozoan parasite responsible for human African trypanosomiasis. Using a rigorous methodology, our analysis led to identification of 128 high-confidence complexes encompassing 716 protein groups, including 635 protein groups that lacked experimental annotation. These complexes correlate well with known pathways as well as for proteins co-expressed across the T. brucei life cycle, and provide potential functions for a large number of previously uncharacterized proteins. We validated the functions of several novel proteins associated with the RNA-editing machinery, identifying a candidate potentially involved in the mitochondrial post-transcriptional regulation of T. brucei. Our data provide an unprecedented view of the protein complex map of T. brucei, and serve as a reliable resource for further characterization of trypanosomatid proteins. The presented results in this study are available at: www.TrypsNetDB.org. |
format | Online Article Text |
id | pubmed-4798371 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-47983712016-03-23 A Protein Complex Map of Trypanosoma brucei Gazestani, Vahid H. Nikpour, Najmeh Mehta, Vaibhav Najafabadi, Hamed S. Moshiri, Houtan Jardim, Armando Salavati, Reza PLoS Negl Trop Dis Research Article The functions of the majority of trypanosomatid-specific proteins are unknown, hindering our understanding of the biology and pathogenesis of Trypanosomatida. While protein-protein interactions are highly informative about protein function, a global map of protein interactions and complexes is still lacking for these important human parasites. Here, benefiting from in-depth biochemical fractionation, we systematically interrogated the co-complex interactions of more than 3354 protein groups in procyclic life stage of Trypanosoma brucei, the protozoan parasite responsible for human African trypanosomiasis. Using a rigorous methodology, our analysis led to identification of 128 high-confidence complexes encompassing 716 protein groups, including 635 protein groups that lacked experimental annotation. These complexes correlate well with known pathways as well as for proteins co-expressed across the T. brucei life cycle, and provide potential functions for a large number of previously uncharacterized proteins. We validated the functions of several novel proteins associated with the RNA-editing machinery, identifying a candidate potentially involved in the mitochondrial post-transcriptional regulation of T. brucei. Our data provide an unprecedented view of the protein complex map of T. brucei, and serve as a reliable resource for further characterization of trypanosomatid proteins. The presented results in this study are available at: www.TrypsNetDB.org. Public Library of Science 2016-03-18 /pmc/articles/PMC4798371/ /pubmed/26991453 http://dx.doi.org/10.1371/journal.pntd.0004533 Text en © 2016 Gazestani et al 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 author and source are credited. |
spellingShingle | Research Article Gazestani, Vahid H. Nikpour, Najmeh Mehta, Vaibhav Najafabadi, Hamed S. Moshiri, Houtan Jardim, Armando Salavati, Reza A Protein Complex Map of Trypanosoma brucei |
title | A Protein Complex Map of Trypanosoma brucei |
title_full | A Protein Complex Map of Trypanosoma brucei |
title_fullStr | A Protein Complex Map of Trypanosoma brucei |
title_full_unstemmed | A Protein Complex Map of Trypanosoma brucei |
title_short | A Protein Complex Map of Trypanosoma brucei |
title_sort | protein complex map of trypanosoma brucei |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4798371/ https://www.ncbi.nlm.nih.gov/pubmed/26991453 http://dx.doi.org/10.1371/journal.pntd.0004533 |
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