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Structural disorder of plasmid-encoded proteins in Bacteria and Archaea
BACKGROUND: In the last decade and a half it has been firmly established that a large number of proteins do not adopt a well-defined (ordered) structure under physiological conditions. Such intrinsically disordered proteins (IDPs) and intrinsically disordered (protein) regions (IDRs) are involved in...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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BioMed Central
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5922023/ https://www.ncbi.nlm.nih.gov/pubmed/29699482 http://dx.doi.org/10.1186/s12859-018-2158-6 |
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author | Mitić, Nenad S. Malkov, Saša N. Kovačević, Jovana J. Pavlović-Lažetić, Gordana M. Beljanski, Miloš V. |
author_facet | Mitić, Nenad S. Malkov, Saša N. Kovačević, Jovana J. Pavlović-Lažetić, Gordana M. Beljanski, Miloš V. |
author_sort | Mitić, Nenad S. |
collection | PubMed |
description | BACKGROUND: In the last decade and a half it has been firmly established that a large number of proteins do not adopt a well-defined (ordered) structure under physiological conditions. Such intrinsically disordered proteins (IDPs) and intrinsically disordered (protein) regions (IDRs) are involved in essential cell processes through two basic mechanisms: the entropic chain mechanism which is responsible for rapid fluctuations among many alternative conformations, and molecular recognition via short recognition elements that bind to other molecules. IDPs possess a high adaptive potential and there is special interest in investigating their involvement in organism evolution. RESULTS: We analyzed 2554 Bacterial and 139 Archaeal proteomes, with a total of 8,455,194 proteins for disorder content and its implications for adaptation of organisms, using three disorder predictors and three measures. Along with other findings, we revealed that for all three predictors and all three measures (1) Bacteria exhibit significantly more disorder than Archaea; (2) plasmid-encoded proteins contain considerably more IDRs than proteins encoded on chromosomes (or whole genomes) in both prokaryote superkingdoms; (3) plasmid proteins are significantly more disordered than chromosomal proteins only in the group of proteins with no COG category assigned; (4) antitoxin proteins in comparison to other proteins, are the most disordered (almost double) in both Bacterial and Archaeal proteomes; (5) plasmidal proteins are more disordered than chromosomal proteins in Bacterial antitoxins and toxin-unclassified proteins, but have almost the same disorder content in toxin proteins. CONCLUSION: Our results suggest that while disorder content depends on genome and proteome characteristics, it is more influenced by functional engagements than by gene location (on chromosome or plasmid). ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12859-018-2158-6) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-5922023 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-59220232018-05-07 Structural disorder of plasmid-encoded proteins in Bacteria and Archaea Mitić, Nenad S. Malkov, Saša N. Kovačević, Jovana J. Pavlović-Lažetić, Gordana M. Beljanski, Miloš V. BMC Bioinformatics Research Article BACKGROUND: In the last decade and a half it has been firmly established that a large number of proteins do not adopt a well-defined (ordered) structure under physiological conditions. Such intrinsically disordered proteins (IDPs) and intrinsically disordered (protein) regions (IDRs) are involved in essential cell processes through two basic mechanisms: the entropic chain mechanism which is responsible for rapid fluctuations among many alternative conformations, and molecular recognition via short recognition elements that bind to other molecules. IDPs possess a high adaptive potential and there is special interest in investigating their involvement in organism evolution. RESULTS: We analyzed 2554 Bacterial and 139 Archaeal proteomes, with a total of 8,455,194 proteins for disorder content and its implications for adaptation of organisms, using three disorder predictors and three measures. Along with other findings, we revealed that for all three predictors and all three measures (1) Bacteria exhibit significantly more disorder than Archaea; (2) plasmid-encoded proteins contain considerably more IDRs than proteins encoded on chromosomes (or whole genomes) in both prokaryote superkingdoms; (3) plasmid proteins are significantly more disordered than chromosomal proteins only in the group of proteins with no COG category assigned; (4) antitoxin proteins in comparison to other proteins, are the most disordered (almost double) in both Bacterial and Archaeal proteomes; (5) plasmidal proteins are more disordered than chromosomal proteins in Bacterial antitoxins and toxin-unclassified proteins, but have almost the same disorder content in toxin proteins. CONCLUSION: Our results suggest that while disorder content depends on genome and proteome characteristics, it is more influenced by functional engagements than by gene location (on chromosome or plasmid). ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12859-018-2158-6) contains supplementary material, which is available to authorized users. BioMed Central 2018-04-25 /pmc/articles/PMC5922023/ /pubmed/29699482 http://dx.doi.org/10.1186/s12859-018-2158-6 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 Article Mitić, Nenad S. Malkov, Saša N. Kovačević, Jovana J. Pavlović-Lažetić, Gordana M. Beljanski, Miloš V. Structural disorder of plasmid-encoded proteins in Bacteria and Archaea |
title | Structural disorder of plasmid-encoded proteins in Bacteria and Archaea |
title_full | Structural disorder of plasmid-encoded proteins in Bacteria and Archaea |
title_fullStr | Structural disorder of plasmid-encoded proteins in Bacteria and Archaea |
title_full_unstemmed | Structural disorder of plasmid-encoded proteins in Bacteria and Archaea |
title_short | Structural disorder of plasmid-encoded proteins in Bacteria and Archaea |
title_sort | structural disorder of plasmid-encoded proteins in bacteria and archaea |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5922023/ https://www.ncbi.nlm.nih.gov/pubmed/29699482 http://dx.doi.org/10.1186/s12859-018-2158-6 |
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