Nuclear Localization Signal of Human Foamy Virus Integrase

인간 포미바이러스 인테그라제의 핵위치 신호

  • Oh Soo-A (Department of Biotechnology and BET Research Institute, Chung-Ang University) ;
  • Kang Seung-Yi (Department of Biotechnology and BET Research Institute, Chung-Ang University) ;
  • Han Sung-Tae (Department of Biotechnology and BET Research Institute, Chung-Ang University) ;
  • An Dog-Gn (Department of Biotechnology and BET Research Institute, Chung-Ang University) ;
  • Shin Cha-Gyun (Department of Biotechnology and BET Research Institute, Chung-Ang University)
  • 오수아 (중앙대학교 산업과학대학 생명공학과, 중앙대학교 생명환경연구원) ;
  • 강승이 (중앙대학교 산업과학대학 생명공학과, 중앙대학교 생명환경연구원) ;
  • 한성태 (중앙대학교 산업과학대학 생명공학과, 중앙대학교 생명환경연구원) ;
  • 안덕근 (중앙대학교 산업과학대학 생명공학과, 중앙대학교 생명환경연구원) ;
  • 신차균 (중앙대학교 산업과학대학 생명공학과, 중앙대학교 생명환경연구원)
  • Published : 2006.04.01

Abstract

Human foamy virus (HFV) integrase mediates integration of viral c-DNA into cellular DNA. In this process, HFV prointegration 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 nuclei, but the mechanisms for nuclear localization of the HFV PIC remains unclear. To functionally identify the NLS of HFV integrase, various subdomains of the protein were expressed as GFP fusions and their subcellular locations were analyzed with confocal laser scanning microscopy. Wild type HFV integrase was karyophilic by targeting the fusion protein to nuclei of the COS-1 and 293T cells. Our results showed that strong NLS of HFV integrase was mapped to the C-terminal regions. In addition the karyophilic properties of N-terminal and central regions are not individually strong enough to direct localization of the fusion proteins to nuclei, but their cooperative activity for nuclear import was confirmed.

Keywords

References

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