Protein Aggregation Profile of the Bacterial Cytosol

• Published in: PloS one Vol. 5; no. 2; p. e9383
• Main Authors: de Groot, Natalia S., Ventura, Salvador
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 25.02.2010; Public Library of Science (PLoS)
• Subjects: Agglomeration; Aggregation behavior; Algorithms; Amino acids; Analysis; Architects; Bacteria; Bacteria - chemistry; Bacteria - metabolism; Bacterial proteins; Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Biochemistry/Bioinformatics; Biotechnology/Protein Chemistry and Proteomics; Coding; Computer applications; Cytosol; Cytosol - metabolism; Databases, Protein; E coli; Escherichia; Escherichia coli; Escherichia coli - chemistry; Escherichia coli - metabolism; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - metabolism; Genomes; Hydrophobic and Hydrophilic Interactions; Microbiology/Microbial Evolution and Genomics; Polypeptides; Protein Conformation; Protein Denaturation; Protein Folding; Protein interaction; Proteins; Proteome - chemistry; Proteome - metabolism; Proteomes; Proteomics; Software; Spain
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0009383

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. 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. 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.