Direct Conversion of an Enzyme from Native-like to Amyloid-like Aggregates within Inclusion Bodies.

ABSTRACT: The acylphosphatase from Sulfolobus solfataricus (Sso AcP) is a globular protein able to aggregate in vitro from a native-like conformational ensemble without the need for a transition across the major unfolding energy barrier. This process leads to the formation of assemblies in which the protein retains its native-like structure, which subsequently convert into amyloid-like aggregates. Here, we investigate the mechanism by which Sso AcP aggregates in vivo to form bacterial inclusion bodies after expression in E. coli. Shortly after the initiation of expression, Sso AcP is incorporated into inclusion bodies as a native-like protein, still exhibiting small but significant enzymatic activity. Additional experiments revealed that this overall process of aggregation is enhanced by the presenc

SUBMITTER: Elia F 

PROVIDER: S-EPMC5479110 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature