title: YY1 is recruited to the cytoplasm of vaccinia virus-infected human macrophages by the Crm1 system.
abstract: The influence of vaccinia virus infection on activity and subcellular localization of cellular transcription factors YY1 and C/EBPbeta in human blood monocytes derived macrophages was examined. YY1 activity, shown by electrophoretic mobility shift assay, decreased upon infection in the nuclear extracts but remained unchanged in whole cell extracts until 48h post-infection (p.i.). Immunohistochemical staining of the fixed cells showed translocation of the factor to the cytoplasm of the infected macrophages. The nuclear export of YY1 was blocked by leptomycin B, an inhibitor of the Crm1-dependent export system. C/EBP DNA binding activity was transiently increased during viral infection. Cytoplasmic translocation of the C/EBPbeta has also been observed and was found to be blocked by leptomycin B treatment of the cells. It appears that the Crm1 system is not impaired by the virus infection in blood-derived macrophages and that it remains operative for redirection of subcellular localization of transcription factors from the nucleus to the cytoplasm. Moreover, blockage of the nuclear export by leptomycin B significantly affected the yield of infectious virus. The results might help to better understand the mechanism of protein transport during viral infection of monocyte-derived cells.
authors.affiliation: Faculty of Biotechnology, Jagiellonian University, 7 Gronostajowa St., 30-387 Krakow, Poland.
authors.forename: Kinga
authors.initials: K
authors.lastname: Slezak
authors.forename: Marta
authors.initials: M
authors.lastname: Michalik
authors.forename: Aleksandra
authors.initials: A
authors.lastname: Kowalczyk
authors.forename: Hanna
authors.initials: H
authors.lastname: Rokita
mesh_terms: D021581:Active Transport, Cell Nucleus; D022782:CCAAT-Enhancer-Binding Protein-beta / Q000378:metabolism*; D002467:Cell Nucleus / Q000378:metabolism; D002478:Cells, Cultured; D003593:Cytoplasm / Q000378:metabolism; D050981:Erythroid-Specific DNA-Binding Factors; D005231:Fatty Acids, Unsaturated / Q000494:pharmacology; D006801:Humans; D007223:Infant; D028884:Karyopherins / Q000502:physiology*; D008264:Macrophages / Q000378:metabolism / Q000821:virology*; D009687:Nuclear Proteins / Q000378:metabolism; D018160:Receptors, Cytoplasmic and Nuclear; D014157:Transcription Factors / Q000378:metabolism*; D014616:Vaccinia virus / Q000254:growth & development*; D014779:Virus Replication; D050986:YY1 Transcription Factor; D000097606:Exportin 1 Protein
chemical_list: D022782:CCAAT-Enhancer-Binding Protein-beta; D050981:Erythroid-Specific DNA-Binding Factors; D005231:Fatty Acids, Unsaturated; D028884:Karyopherins; D009687:Nuclear Proteins; D018160:Receptors, Cytoplasmic and Nuclear; D014157:Transcription Factors; D050986:YY1 Transcription Factor; D000097606:Exportin 1 Protein; C494698:YY1 protein, human; C038753:leptomycin B