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Protein Aggregation Profile of the Bacterial Cytosol
BACKGROUND: Protein misfolding is usually deleterious for the cell, either as a consequence of the loss of protein function or the buildup of insoluble and toxic aggregates. The aggregation behavior of a given polypeptide is strongly influenced by the intrinsic properties encoded in its sequence. Th...
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Formato: | Texto |
Lenguaje: | English |
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Public Library of Science
2010
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2828471/ https://www.ncbi.nlm.nih.gov/pubmed/20195530 http://dx.doi.org/10.1371/journal.pone.0009383 |
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author | de Groot, Natalia S. Ventura, Salvador |
author_facet | de Groot, Natalia S. Ventura, Salvador |
author_sort | de Groot, Natalia S. |
collection | PubMed |
description | BACKGROUND: Protein misfolding is usually deleterious for the cell, either as a consequence of the loss of protein function or the buildup of insoluble and toxic aggregates. The aggregation behavior of a given polypeptide is strongly influenced by the intrinsic properties encoded in its sequence. This has allowed the development of effective computational methods to predict protein aggregation propensity. METHODOLOGY/PRINCIPAL FINDINGS: Here, we use the AGGRESCAN algorithm to approximate the aggregation profile of an experimental cytosolic Escherichia coli proteome. The analysis indicates that the aggregation propensity of bacterial proteins is associated with their length, conformation, location, function, and abundance. The data are consistent with the predictions of other algorithms on different theoretical proteomes. CONCLUSIONS/SIGNIFICANCE: Overall, the study suggests that the avoidance of protein aggregation in functional environments acts as a strong evolutionary constraint on polypeptide sequences in both prokaryotic and eukaryotic organisms. |
format | Text |
id | pubmed-2828471 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-28284712010-03-02 Protein Aggregation Profile of the Bacterial Cytosol de Groot, Natalia S. Ventura, Salvador PLoS One Research Article BACKGROUND: Protein misfolding is usually deleterious for the cell, either as a consequence of the loss of protein function or the buildup of insoluble and toxic aggregates. The aggregation behavior of a given polypeptide is strongly influenced by the intrinsic properties encoded in its sequence. This has allowed the development of effective computational methods to predict protein aggregation propensity. METHODOLOGY/PRINCIPAL FINDINGS: Here, we use the AGGRESCAN algorithm to approximate the aggregation profile of an experimental cytosolic Escherichia coli proteome. The analysis indicates that the aggregation propensity of bacterial proteins is associated with their length, conformation, location, function, and abundance. The data are consistent with the predictions of other algorithms on different theoretical proteomes. CONCLUSIONS/SIGNIFICANCE: Overall, the study suggests that the avoidance of protein aggregation in functional environments acts as a strong evolutionary constraint on polypeptide sequences in both prokaryotic and eukaryotic organisms. Public Library of Science 2010-02-25 /pmc/articles/PMC2828471/ /pubmed/20195530 http://dx.doi.org/10.1371/journal.pone.0009383 Text en de Groot, Ventura. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article de Groot, Natalia S. Ventura, Salvador Protein Aggregation Profile of the Bacterial Cytosol |
title | Protein Aggregation Profile of the Bacterial Cytosol |
title_full | Protein Aggregation Profile of the Bacterial Cytosol |
title_fullStr | Protein Aggregation Profile of the Bacterial Cytosol |
title_full_unstemmed | Protein Aggregation Profile of the Bacterial Cytosol |
title_short | Protein Aggregation Profile of the Bacterial Cytosol |
title_sort | protein aggregation profile of the bacterial cytosol |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2828471/ https://www.ncbi.nlm.nih.gov/pubmed/20195530 http://dx.doi.org/10.1371/journal.pone.0009383 |
work_keys_str_mv | AT degrootnatalias proteinaggregationprofileofthebacterialcytosol AT venturasalvador proteinaggregationprofileofthebacterialcytosol |