Mapping of the APE1 domains responsible for GSNO-induced nuclear export

Abstract

<p><b>Copyright information:</b></p><p>Taken from "Nitric oxide controls nuclear export of APE1/Ref-1 through S-nitrosation of Cysteines 93 and 310"</p><p></p><p>Nucleic Acids Research 2007;35(8):2522-2532.</p><p>Published online 1 Apr 2007</p><p>PMCID:PMC1885639.</p><p>© 2007 The Author(s)</p> () Immunofluorescence images depicting the subcellular localization of APE1 truncated mutants in transfected HEK293 cells. () Schematic representation of the N-terminal and C-terminal truncated mutants of APE1. The NLS and the predicted NES and MTS within the full-length protein are indicated. C, cytoplasmic staining; N, nuclear staining; M, mitochondrial staining. () The subcellular distribution of HA-APE1(Δ64-80) and HA-APE1(1-305) determined by immunofluorescence in the presence of GSNO treatment. () Three-dimensional localization of the B1 (amino acids 61–69) and B2 (amino acids 311–317) beta-strands and the S-nitrosation sites C93 and C310 in the closed conformation of APE1. B1 and B2 form an antiparallel beta-fold. C93 and C310 are close to B1 and B2, respectively