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Protein aggregation profile of the bacterial cytosol
Sánchez de Groot, Natalia (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
Ventura Zamora, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)

Data: 2010
Resum: 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.
Drets: Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, fins i tot amb finalitats comercials, sempre i quan es reconegui l'autoria de l'obra original. Creative Commons
Llengua: Anglès.
Document: article ; publishedVersion
Matèria: Proteïnes ; Agregació ; Escherichia coli ; Protein aggregation
Publicat a: PLoS one, Vol. 5, N. 2 (February 2010) , p. e9383, ISSN 1932-6203

DOI: 10.1371/journal.pone.0009383

17 p, 1.6 MB

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