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Success: evolutionary and structural properties of amino acids prove effective for succinylation site prediction
BACKGROUND: Post-translational modification is considered an important biological mechanism with critical impact on the diversification of the proteome. Although a long list of such modifications has been studied, succinylation of lysine residues has recently attracted the interest of the scientific...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5781056/ https://www.ncbi.nlm.nih.gov/pubmed/29363424 http://dx.doi.org/10.1186/s12864-017-4336-8 |
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author | López, Yosvany Sharma, Alok Dehzangi, Abdollah Lal, Sunil Pranit Taherzadeh, Ghazaleh Sattar, Abdul Tsunoda, Tatsuhiko |
author_facet | López, Yosvany Sharma, Alok Dehzangi, Abdollah Lal, Sunil Pranit Taherzadeh, Ghazaleh Sattar, Abdul Tsunoda, Tatsuhiko |
author_sort | López, Yosvany |
collection | PubMed |
description | BACKGROUND: Post-translational modification is considered an important biological mechanism with critical impact on the diversification of the proteome. Although a long list of such modifications has been studied, succinylation of lysine residues has recently attracted the interest of the scientific community. The experimental detection of succinylation sites is an expensive process, which consumes a lot of time and resources. Therefore, computational predictors of this covalent modification have emerged as a last resort to tackling lysine succinylation. RESULTS: In this paper, we propose a novel computational predictor called ‘Success’, which efficiently uses the structural and evolutionary information of amino acids for predicting succinylation sites. To do this, each lysine was described as a vector that combined the above information of surrounding amino acids. We then designed a support vector machine with a radial basis function kernel for discriminating between succinylated and non-succinylated residues. We finally compared the Success predictor with three state-of-the-art predictors in the literature. As a result, our proposed predictor showed a significant improvement over the compared predictors in statistical metrics, such as sensitivity (0.866), accuracy (0.838) and Matthews correlation coefficient (0.677) on a benchmark dataset. CONCLUSIONS: The proposed predictor effectively uses the structural and evolutionary information of the amino acids surrounding a lysine. The bigram feature extraction approach, while retaining the same number of features, facilitates a better description of lysines. A support vector machine with a radial basis function kernel was used to discriminate between modified and unmodified lysines. The aforementioned aspects make the Success predictor outperform three state-of-the-art predictors in succinylation detection. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12864-017-4336-8) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-5781056 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-57810562018-02-06 Success: evolutionary and structural properties of amino acids prove effective for succinylation site prediction López, Yosvany Sharma, Alok Dehzangi, Abdollah Lal, Sunil Pranit Taherzadeh, Ghazaleh Sattar, Abdul Tsunoda, Tatsuhiko BMC Genomics Research BACKGROUND: Post-translational modification is considered an important biological mechanism with critical impact on the diversification of the proteome. Although a long list of such modifications has been studied, succinylation of lysine residues has recently attracted the interest of the scientific community. The experimental detection of succinylation sites is an expensive process, which consumes a lot of time and resources. Therefore, computational predictors of this covalent modification have emerged as a last resort to tackling lysine succinylation. RESULTS: In this paper, we propose a novel computational predictor called ‘Success’, which efficiently uses the structural and evolutionary information of amino acids for predicting succinylation sites. To do this, each lysine was described as a vector that combined the above information of surrounding amino acids. We then designed a support vector machine with a radial basis function kernel for discriminating between succinylated and non-succinylated residues. We finally compared the Success predictor with three state-of-the-art predictors in the literature. As a result, our proposed predictor showed a significant improvement over the compared predictors in statistical metrics, such as sensitivity (0.866), accuracy (0.838) and Matthews correlation coefficient (0.677) on a benchmark dataset. CONCLUSIONS: The proposed predictor effectively uses the structural and evolutionary information of the amino acids surrounding a lysine. The bigram feature extraction approach, while retaining the same number of features, facilitates a better description of lysines. A support vector machine with a radial basis function kernel was used to discriminate between modified and unmodified lysines. The aforementioned aspects make the Success predictor outperform three state-of-the-art predictors in succinylation detection. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12864-017-4336-8) contains supplementary material, which is available to authorized users. BioMed Central 2018-01-19 /pmc/articles/PMC5781056/ /pubmed/29363424 http://dx.doi.org/10.1186/s12864-017-4336-8 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 López, Yosvany Sharma, Alok Dehzangi, Abdollah Lal, Sunil Pranit Taherzadeh, Ghazaleh Sattar, Abdul Tsunoda, Tatsuhiko Success: evolutionary and structural properties of amino acids prove effective for succinylation site prediction |
title | Success: evolutionary and structural properties of amino acids prove effective for succinylation site prediction |
title_full | Success: evolutionary and structural properties of amino acids prove effective for succinylation site prediction |
title_fullStr | Success: evolutionary and structural properties of amino acids prove effective for succinylation site prediction |
title_full_unstemmed | Success: evolutionary and structural properties of amino acids prove effective for succinylation site prediction |
title_short | Success: evolutionary and structural properties of amino acids prove effective for succinylation site prediction |
title_sort | success: evolutionary and structural properties of amino acids prove effective for succinylation site prediction |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5781056/ https://www.ncbi.nlm.nih.gov/pubmed/29363424 http://dx.doi.org/10.1186/s12864-017-4336-8 |
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