Changes in biophysical characteristics of PFN1 due to mutation causing amyotrophic lateral sclerosis.

ABSTRACT: Single amino acid mutations in profilin 1 (PFN1) have been found to cause amyotrophic lateral sclerosis (ALS). Recently, we developed a mouse model for ALS using a PFN1 mutation (glycine 118 to valine, G118V), and we are now interested in understanding how PFN1 becomes toxically lethal with only one amino acid substitution. Therefore, we studied mutation-related changes in the PFN1 protein and hypothesized that such changes significantly disturb its structure. Initially, we expressed and studied the purified PFN1^WT and PFN1^G118V proteins from bacterial culture. We found that the PFN1^G118V protein has a different mean residue ellipticity, as measured by far-UV circular dichroism, accompanied by a spectral shift. The intrinsic fluorescence of PFN1^G118V</

SUBMITTER: Nekouei M 

PROVIDER: S-EPMC6230493 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature