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Identifying binary protein-protein interactions from affinity purification mass spectrometry data

BACKGROUND: The identification of protein-protein interactions contributes greatly to the understanding of functional organization within cells. With the development of affinity purification-mass spectrometry (AP-MS) techniques, several computational scoring methods have been proposed to detect prot...

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Autores principales: Zhang, Xiao-Fei, Ou-Yang, Le, Hu, Xiaohua, Dai, Dao-Qing
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4595009/
https://www.ncbi.nlm.nih.gov/pubmed/26438428
http://dx.doi.org/10.1186/s12864-015-1944-z
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author Zhang, Xiao-Fei
Ou-Yang, Le
Hu, Xiaohua
Dai, Dao-Qing
author_facet Zhang, Xiao-Fei
Ou-Yang, Le
Hu, Xiaohua
Dai, Dao-Qing
author_sort Zhang, Xiao-Fei
collection PubMed
description BACKGROUND: The identification of protein-protein interactions contributes greatly to the understanding of functional organization within cells. With the development of affinity purification-mass spectrometry (AP-MS) techniques, several computational scoring methods have been proposed to detect protein interactions from AP-MS data. However, most of the current methods focus on the detection of co-complex interactions and do not discriminate between direct physical interactions and indirect interactions. Consequently, less is known about the precise physical wiring diagram within cells. RESULTS: In this paper, we develop a Binary Interaction Network Model (BINM) to computationally identify direct physical interactions from co-complex interactions which can be inferred from purification data using previous scoring methods. This model provides a mathematical framework for capturing topological relationships between direct physical interactions and observed co-complex interactions. It reassigns a confidence score to each observed interaction to indicate its propensity to be a direct physical interaction. Then observed interactions with high confidence scores are predicted as direct physical interactions. We run our model on two yeast co-complex interaction networks which are constructed by two different scoring methods on a same combined AP-MS data. The direct physical interactions identified by various methods are comprehensively benchmarked against different reference sets that provide both direct and indirect evidence for physical contacts. Experiment results show that our model has a competitive performance over the state-of-the-art methods. CONCLUSIONS: According to the results obtained in this study, BINM is a powerful scoring method that can solely use network topology to predict direct physical interactions from AP-MS data. This study provides us an alternative approach to explore the information inherent in AP-MS data. The software can be downloaded from https://github.com/Zhangxf-ccnu/BINM. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12864-015-1944-z) contains supplementary material, which is available to authorized users.
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spelling pubmed-45950092015-10-07 Identifying binary protein-protein interactions from affinity purification mass spectrometry data Zhang, Xiao-Fei Ou-Yang, Le Hu, Xiaohua Dai, Dao-Qing BMC Genomics Research Article BACKGROUND: The identification of protein-protein interactions contributes greatly to the understanding of functional organization within cells. With the development of affinity purification-mass spectrometry (AP-MS) techniques, several computational scoring methods have been proposed to detect protein interactions from AP-MS data. However, most of the current methods focus on the detection of co-complex interactions and do not discriminate between direct physical interactions and indirect interactions. Consequently, less is known about the precise physical wiring diagram within cells. RESULTS: In this paper, we develop a Binary Interaction Network Model (BINM) to computationally identify direct physical interactions from co-complex interactions which can be inferred from purification data using previous scoring methods. This model provides a mathematical framework for capturing topological relationships between direct physical interactions and observed co-complex interactions. It reassigns a confidence score to each observed interaction to indicate its propensity to be a direct physical interaction. Then observed interactions with high confidence scores are predicted as direct physical interactions. We run our model on two yeast co-complex interaction networks which are constructed by two different scoring methods on a same combined AP-MS data. The direct physical interactions identified by various methods are comprehensively benchmarked against different reference sets that provide both direct and indirect evidence for physical contacts. Experiment results show that our model has a competitive performance over the state-of-the-art methods. CONCLUSIONS: According to the results obtained in this study, BINM is a powerful scoring method that can solely use network topology to predict direct physical interactions from AP-MS data. This study provides us an alternative approach to explore the information inherent in AP-MS data. The software can be downloaded from https://github.com/Zhangxf-ccnu/BINM. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12864-015-1944-z) contains supplementary material, which is available to authorized users. BioMed Central 2015-10-05 /pmc/articles/PMC4595009/ /pubmed/26438428 http://dx.doi.org/10.1186/s12864-015-1944-z Text en © Zhang et al. 2015 Open Access This 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 Article
Zhang, Xiao-Fei
Ou-Yang, Le
Hu, Xiaohua
Dai, Dao-Qing
Identifying binary protein-protein interactions from affinity purification mass spectrometry data
title Identifying binary protein-protein interactions from affinity purification mass spectrometry data
title_full Identifying binary protein-protein interactions from affinity purification mass spectrometry data
title_fullStr Identifying binary protein-protein interactions from affinity purification mass spectrometry data
title_full_unstemmed Identifying binary protein-protein interactions from affinity purification mass spectrometry data
title_short Identifying binary protein-protein interactions from affinity purification mass spectrometry data
title_sort identifying binary protein-protein interactions from affinity purification mass spectrometry data
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4595009/
https://www.ncbi.nlm.nih.gov/pubmed/26438428
http://dx.doi.org/10.1186/s12864-015-1944-z
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