title: Minimal size of prototype foamy virus integrase for nuclear localization.
abstract: We have reported previously that the prototype foamy virus (PFV) integrase (IN) has a strong nuclear localization signal (NLS) in its C-terminal domain, in particular in a region of aa 306-334 including highly karyophilic arginines or lysines at positions 308, 313, 318, 324, and 329. In this study, we used various mutants of the C-terminal domain to further analyze its karyophilic determinants. Plasmids expressing these mutants fused to maltose binding protein (MBP) and enhanced green fluorescent protein (EGFP) were transfected to COS-1 cells and subcellular localization of these fluorescent fusion proteins was determined by fluorescent microscopy. The results revealed that a maximum karyophilicity was exhibited by a region longer than the previously described one of 29 aa (aa 306-334), in particular by a 64 aa region (aa 289-352) with Arg341 and Lys349 as critical determinants.
authors.affiliation: Department of Biotechnology, Chung-Ang University, Ansung 456-756, South Korea.
authors.forename: U
authors.initials: U
authors.lastname: Hyun
authors.forename: D H
authors.initials: DH
authors.lastname: Lee
authors.forename: C G
authors.initials: CG
authors.lastname: Shin
mesh_terms: D021581:Active Transport, Cell Nucleus; D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D002467:Cell Nucleus / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics; D006801:Humans; D019426:Integrases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D019913:Nuclear Localization Signals; D017434:Protein Structure, Tertiary; D012192:Retroviridae Infections / Q000821:virology*; D016092:Spumavirus / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D019913:Nuclear Localization Signals; D014764:Viral Proteins; D019426:Integrases