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fLPS: Fast discovery of compositional biases for the protein universe
BACKGROUND: Proteins often contain regions that are compositionally biased (CB), i.e., they are made from a small subset of amino-acid residue types. These CB regions can be functionally important, e.g., the prion-forming and prion-like regions that are rich in asparagine and glutamine residues. RES...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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BioMed Central
2017
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5684748/ https://www.ncbi.nlm.nih.gov/pubmed/29132292 http://dx.doi.org/10.1186/s12859-017-1906-3 |
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author | Harrison, Paul M. |
author_facet | Harrison, Paul M. |
author_sort | Harrison, Paul M. |
collection | PubMed |
description | BACKGROUND: Proteins often contain regions that are compositionally biased (CB), i.e., they are made from a small subset of amino-acid residue types. These CB regions can be functionally important, e.g., the prion-forming and prion-like regions that are rich in asparagine and glutamine residues. RESULTS: Here I report a new program fLPS that can rapidly annotate CB regions. It discovers both single-residue and multiple-residue biases. It works through a process of probability minimization. First, contigs are constructed for each amino-acid type out of sequence windows with a low degree of bias; second, these contigs are searched exhaustively for low-probability subsequences (LPSs); third, such LPSs are iteratively assessed for merger into possible multiple-residue biases. At each of these stages, efficiency measures are taken to avoid or delay probability calculations unless/until they are necessary. On a current desktop workstation, the fLPS algorithm can annotate the biased regions of the yeast proteome (>5700 sequences) in <1 s, and of the whole current TrEMBL database (>65 million sequences) in as little as ~1 h, which is >2 times faster than the commonly used program SEG, using default parameters. fLPS discovers both shorter CB regions (of the sort that are often termed ‘low-complexity sequence’), and milder biases that may only be detectable over long tracts of sequence. CONCLUSIONS: fLPS can readily handle very large protein data sets, such as might come from metagenomics projects. It is useful in searching for proteins with similar CB regions, and for making functional inferences about CB regions for a protein of interest. The fLPS package is available from: http://biology.mcgill.ca/faculty/harrison/flps.html, or https://github.com/pmharrison/flps, or is a supplement to this article. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12859-017-1906-3) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-5684748 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-56847482017-11-20 fLPS: Fast discovery of compositional biases for the protein universe Harrison, Paul M. BMC Bioinformatics Software BACKGROUND: Proteins often contain regions that are compositionally biased (CB), i.e., they are made from a small subset of amino-acid residue types. These CB regions can be functionally important, e.g., the prion-forming and prion-like regions that are rich in asparagine and glutamine residues. RESULTS: Here I report a new program fLPS that can rapidly annotate CB regions. It discovers both single-residue and multiple-residue biases. It works through a process of probability minimization. First, contigs are constructed for each amino-acid type out of sequence windows with a low degree of bias; second, these contigs are searched exhaustively for low-probability subsequences (LPSs); third, such LPSs are iteratively assessed for merger into possible multiple-residue biases. At each of these stages, efficiency measures are taken to avoid or delay probability calculations unless/until they are necessary. On a current desktop workstation, the fLPS algorithm can annotate the biased regions of the yeast proteome (>5700 sequences) in <1 s, and of the whole current TrEMBL database (>65 million sequences) in as little as ~1 h, which is >2 times faster than the commonly used program SEG, using default parameters. fLPS discovers both shorter CB regions (of the sort that are often termed ‘low-complexity sequence’), and milder biases that may only be detectable over long tracts of sequence. CONCLUSIONS: fLPS can readily handle very large protein data sets, such as might come from metagenomics projects. It is useful in searching for proteins with similar CB regions, and for making functional inferences about CB regions for a protein of interest. The fLPS package is available from: http://biology.mcgill.ca/faculty/harrison/flps.html, or https://github.com/pmharrison/flps, or is a supplement to this article. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12859-017-1906-3) contains supplementary material, which is available to authorized users. BioMed Central 2017-11-13 /pmc/articles/PMC5684748/ /pubmed/29132292 http://dx.doi.org/10.1186/s12859-017-1906-3 Text en © The Author(s). 2017 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 | Software Harrison, Paul M. fLPS: Fast discovery of compositional biases for the protein universe |
title | fLPS: Fast discovery of compositional biases for the protein universe |
title_full | fLPS: Fast discovery of compositional biases for the protein universe |
title_fullStr | fLPS: Fast discovery of compositional biases for the protein universe |
title_full_unstemmed | fLPS: Fast discovery of compositional biases for the protein universe |
title_short | fLPS: Fast discovery of compositional biases for the protein universe |
title_sort | flps: fast discovery of compositional biases for the protein universe |
topic | Software |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5684748/ https://www.ncbi.nlm.nih.gov/pubmed/29132292 http://dx.doi.org/10.1186/s12859-017-1906-3 |
work_keys_str_mv | AT harrisonpaulm flpsfastdiscoveryofcompositionalbiasesfortheproteinuniverse |