title: Adenovirus early region 4 34-kilodalton protein directs the nuclear localization of the early region 1B 55-kilodalton protein in primate cells.
abstract: The localization of the adenovirus type 5 34-kDa E4 and 55-kDa E1B proteins was determined in the absence of other adenovirus proteins. When expressed by transfection in human, monkey, hamster, rat, and mouse cell lines, the E1B protein was predominantly cytoplasmic and typically was excluded from the nucleus. When expressed by transfection, the E4 protein accumulated in the nucleus. Strikingly, when coexpressed by transfection in human, monkey, or baby hamster kidney cells, the E1B protein colocalized in the nucleus with the E4 protein. A complex of the E4 and E1B proteins was identified by coimmunoprecipitation in transfected HeLa cells. By contrast to the interaction observed in primate and baby hamster kidney cells, the E4 protein failed to direct the E1B protein to the nucleus in rat and mouse cell lines as well as CHO and V79 hamster cell lines. This failure of the E4 protein to direct the nuclear localization of the E1B protein in REF-52 rat cells was overcome by fusion with HeLa cells. Within 4 h of heterokaryon formation and with protein synthesis inhibited, a portion of the E4 protein present in the REF-52 nuclei migrated to the HeLa nuclei. Simultaneously, the previously cytoplasmic E1B protein colocalized with the E4 protein in both human and rat cell nuclei. These results suggest that a primate cell-specific factor mediates the functional interaction of the E1B and E4 proteins of adenovirus.
authors.affiliation: Molecular Genetics Program, Bowman Gray School of Medicine, Wake Forest University, Winston-Salem, North Carolina 27157-1064, USA.
authors.forename: F D
authors.initials: FD
authors.lastname: Goodrum
authors.forename: T
authors.initials: T
authors.lastname: Shenk
authors.forename: D A
authors.initials: DA
authors.lastname: Ornelles
mesh_terms: D016475:3T3 Cells; D017501:Adenovirus E1B Proteins / Q000032:analysis / Q000096:biosynthesis*; D017504:Adenovirus E4 Proteins / Q000096:biosynthesis / Q000502:physiology*; D000260:Adenoviruses, Human / Q000502:physiology*; D000818:Animals; D001483:Base Sequence; D016466:CHO Cells; D002460:Cell Line; D002467:Cell Nucleus / Q000378:metabolism / Q000821:virology*; D002522:Chlorocebus aethiops; D003001:Cloning, Molecular; D006224:Cricetinae; D019084:Fluorescent Antibody Technique, Indirect; D006367:HeLa Cells; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009838:Oligodeoxyribonucleotides; D011323:Primates; D051381:Rats; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000378:metabolism; D015183:Restriction Mapping; D013045:Species Specificity; D014709:Vero Cells
chemical_list: D017501:Adenovirus E1B Proteins; D017504:Adenovirus E4 Proteins; D009838:Oligodeoxyribonucleotides; D011994:Recombinant Proteins