YAKHAK HOEJI (약학회지)

The Pharmaceutical Society of Korea (대한약학회)
권호 표지

Characterization of Human Foamy Virus Integrase Mutant

인간 포미바이러스 인테그라제 돌연변이의 특성

  • Kang Seung Yi (Department of Biotechnology and BET Research Institute, Chung-Ang University) ;
  • Oh Soo A (Department of Biotechnology and BET Research Institute, Chung-Ang University) ;
  • Lee Hak Sung (Department of Biotechnology and BET Research Institute, Chung-Ang University) ;
  • Han Sung Tai (Department of Biotechnology and BET Research Institute, Chung-Ang University) ;
  • Shin Cha-Gyun (Department of Biotechnology and BET Research Institute, Chung-Ang University)
  • 강승이 (중앙대학교 산업과학대학 생명공학과) ;
  • 오수아 (중앙대학교 산업과학대학 생명공학과) ;
  • 이학성 (중앙대학교 산업과학대학 생명공학과) ;
  • 한성태 (중앙대학교 산업과학대학 생명공학과) ;
  • 신차균 (중앙대학교 생명환경연구원)
  • Published : 2005.06.01
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Abstract

Human foamy virus (HFV) integrase mediates integration of viral c-DNA into cellular DNA. In this process, HFV integrase recognizes its own viral DNA specifically and catalyzes insertion of viral c-DNA. In order to study catalytic domains and residues, three deletion mutants and two point mutants of HFV integrase were constructed and analyzed with respect to enzymatic activities. The C-terminal deletion mutant showed decreased enzymatic activities while the N-terminal deletion mutant lost the activities completely, indicating that the N-terminal domain is more important than the C-terminal domain in enzymatic reaction. The point mutants, in which an aspartic acid at the 164th position or a glutamic acid at the 200th position of the HFV integrase protein was changed to an alanine, lost the enzymatic activities completely. However, they were well complemented with other defective deletion mutants to recover enzymatic activities partially. Therefore, these results suggest that the aspartic acid and glutamic acid at the respective 164th and 200th positions are catalytic residues for enzymatic reaction.

Keywords

References

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