Expression, purification and characterization of soluble red rooster laforin as a fusion protein in Escherichia coli.

ABSTRACT:

Background

The gene that encodes laforin, a dual-specificity phosphatase with a carbohydrate-binding module, is mutated in Lafora disease (LD). LD is an autosomal recessive, fatal progressive myoclonus epilepsy characterized by the intracellular buildup of insoluble, hyperphosphorylated glycogen-like particles, called Lafora bodies. Laforin dephosphorylates glycogen and other glucans in vitro, but the structural basis of its activity remains unknown. Recombinant human laforin when expressed in and purified from E. coli is largely insoluble and prone to aggregation and precipitation. Identification of a laforin ortholog that is more soluble and stable in vitro would circumvent this issue.

Results

In this study, we cloned multiple laforin orthologs, established a purification

SUBMITTER: Brewer MK 

PROVIDER: S-EPMC4234410 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature