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오수아(Soo A Oh),강승이(Seung Yi Kang),한성태(Sung Tae Han),안덕근(Dog Gn An),신차균(Cha-Gyun Shin) 대한약학회 2006 약학회지 Vol.50 No.2
Human foamy virus (HFV) integrase mediates integration of viral c-DNA into cellular DNA. In this process, HFV preintegration complex (PIC) in which integrase is a key component moves to nuclei of the infected cells and leads to integration of viral DNA to the cellular genome, which is essential in viral life cycle. In general nuclear localization signals (NLS) have been suggested to be involved in localizing retroviral PIC to muclei, but the mechanisms for nuclear localization of the HFV PIC remains unclear. To functionally identufy the NLS of HFV integrase, various subdomains of the protein were expressed as GFP fusions and fusions and their subcellular locations were analyzed with comfocal laser scanning microscopy. Wild type HFV integrase was karyophilic by targeting the fusion protein to nuclei of the COS-1 and 294T cells. Our results showed that strong NLS of HFV integrase was mapped to the C-terminal regions. In addition the karyophimic properties of N-ter- minal and central regions are not individually strong enough to direct localization of the fusion proteins to nuclei, but their cooperative activity for nuclear inport was comfirmed.