title: Protein activity in bacterial inclusion bodies correlates with predicted aggregation rates.
abstract: Recent data show that protein aggregation as bacterial inclusion bodies does not necessarily imply loss of biological activity. Here, we investigate the effect of a large set of single-point mutants of an aggregation-prone protein on its specific activity once deposited in inclusion bodies. The activity of such aggregates significantly correlates with the predicted aggregation rates for each mutant, suggesting that rationally tuning the kinetic competition between folding and aggregation might result in highly active, inclusion bodies. The exploration of this technology during recombinant protein production would have a significant biotechnological value.
authors.affiliation: Departament de Bioquímica i Biologia Molecular, Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, E-08193 Bellaterra, Spain.
authors.forename: Natalia Sánchez
authors.initials: NS
authors.lastname: de Groot
authors.forename: Salvador
authors.initials: S
authors.lastname: Ventura
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D002479:Inclusion Bodies / Q000737:chemistry / Q000378:metabolism* / Q000502:physiology; D007700:Kinetics; D008856:Microscopy, Fluorescence; D011489:Protein Denaturation; D017510:Protein Folding; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012995:Solubility
chemical_list: D001426:Bacterial Proteins; D011993:Recombinant Fusion Proteins