Structural and functional analysis of single-nucleotide polymorphic variants of purine-rich element-binding protein B.

ABSTRACT: Purine-rich element-binding protein B (Purβ) inhibits myofibroblast differentiation by repressing the expression of the smooth muscle α-actin gene (Acta2). Several reports have identified the structural domains in Purβ that enable its characteristic interaction with purine-rich single-stranded DNA (ssDNA) sequences in the Acta2 promoter. However, little is known about the physical and functional effects of single-nucleotide polymorphisms that alter individual amino acid residues in Purβ. This study evaluated seven rare single amino acid variants of human PURB engineered into the homologous mouse Purβ protein. Mapping the location of variant residues on a homology model of the Purβ homodimer suggested that most of the altered residues are remote from the predicted ssDNA-binding regions of t

SUBMITTER: Ferris LA 

PROVIDER: S-EPMC6382573 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature