Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant.

ABSTRACT: Small organic molecules termed osmolytes are harnessed by a variety of cell types in a wide range of organisms to counter unfavorable physiological conditions that challenge protein stability and function. Using a well characterized reporter system that we developed to allow in vivo observations, we have explored how the osmolyte proline influences the stability and aggregation of a model aggregation-prone protein, P39A cellular retinoic acid-binding protein. Strikingly, we find that the natural osmolyte proline abrogates aggregation both in vitro and in vivo (in an Escherichia coli expression system). Importantly, proline also prevented aggregation of constructs containing exon 1 of huntingtin with extended polyglutamine tracts. Although compatible osmolytes are known to stabilize the nat

SUBMITTER: Ignatova Z 

PROVIDER: S-EPMC1569168 | biostudies-literature | 2006 Sep

REPOSITORIES: biostudies-literature