ZBP1 subcellular localization and association with stress granules is controlled by its Z-DNA binding domains.

ABSTRACT: Z-DNA binding protein 1 (ZBP1) belongs to a family of proteins that contain the Zalpha domain, which binds specifically to left-handed Z-DNA and Z-RNA. Like all vertebrate proteins in the Zalpha family, it contains two Zalpha-like domains and is highly inducible by immunostimulation. Using circular dichroism spectroscopy and electrophoretic mobility shift assays we show that both Zalpha domains can bind Z-DNA independently and that substrate binding is greatly enhanced when both domains are linked. Full length ZBP1 and a prominent splice variant lacking the first Zalpha domain (DeltaZalpha) showed strikingly different subcellular localizations. While the full length protein showed a finely punctate cytoplasmatic distribution, ZBP1DeltaZalpha accumulated in large cytoplasmic granules. Mutat

SUBMITTER: Deigendesch N 

PROVIDER: S-EPMC1636418 | biostudies-literature | 2006

REPOSITORIES: biostudies-literature