Structural disorder of plasmid-encoded proteins in Bacteria and Archaea
Abstract 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 inv...
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| Format: | Article |
| Language: | English |
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BMC
2018-04-01
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| Series: | BMC Bioinformatics |
| Subjects: | |
| Online Access: | http://link.springer.com/article/10.1186/s12859-018-2158-6 |
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| author | Nenad S. Mitić Saša N. Malkov Jovana J. Kovačević Gordana M. Pavlović-Lažetić Miloš V. Beljanski |
| author_facet | Nenad S. Mitić Saša N. Malkov Jovana J. Kovačević Gordana M. Pavlović-Lažetić Miloš V. Beljanski |
| author_sort | Nenad S. Mitić |
| collection | DOAJ |
| description | Abstract 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). |
| first_indexed | 2024-04-12T07:25:15Z |
| format | Article |
| id | doaj.art-c90680fe7a7e47998f262b94edbd3b54 |
| institution | Directory Open Access Journal |
| issn | 1471-2105 |
| language | English |
| last_indexed | 2024-04-12T07:25:15Z |
| publishDate | 2018-04-01 |
| publisher | BMC |
| record_format | Article |
| series | BMC Bioinformatics |
| spelling | doaj.art-c90680fe7a7e47998f262b94edbd3b542022-12-22T03:42:13ZengBMCBMC Bioinformatics1471-21052018-04-0119111810.1186/s12859-018-2158-6Structural disorder of plasmid-encoded proteins in Bacteria and ArchaeaNenad S. Mitić0Saša N. Malkov1Jovana J. Kovačević2Gordana M. Pavlović-Lažetić3Miloš V. Beljanski4Department of Computer Science, Faculty of Mathematics, University of BelgradeDepartment of Computer Science, Faculty of Mathematics, University of BelgradeDepartment of Computer Science, Faculty of Mathematics, University of BelgradeDepartment of Computer Science, Faculty of Mathematics, University of BelgradeBio-lab, Institute of General and Physical ChemistryAbstract 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).http://link.springer.com/article/10.1186/s12859-018-2158-6Intrinsically disordered proteinsPlasmid-encoded proteinsToxin/antitoxinBacteria and Archaea |
| spellingShingle | Nenad S. Mitić Saša N. Malkov Jovana J. Kovačević Gordana M. Pavlović-Lažetić Miloš V. Beljanski Structural disorder of plasmid-encoded proteins in Bacteria and Archaea BMC Bioinformatics Intrinsically disordered proteins Plasmid-encoded proteins Toxin/antitoxin 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 | Intrinsically disordered proteins Plasmid-encoded proteins Toxin/antitoxin Bacteria and Archaea |
| url | http://link.springer.com/article/10.1186/s12859-018-2158-6 |
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