인간 포미바이러스 인테그라제 돌연변이의 특성

• 영문명: Characterization of Human Foamy Virus Integrase Mutant
• 발행기관: 대한약학회
• 저자명: 강승이(Seung Yi Kang) 오수아(Soo A Oh) 이학성(Hak Sung Lee) 한성태(Sung Tai Han) 신차균(Cha-Gyun Shin)
• 간행물 정보: 『약학회지』제49권 제3호 (2005년), 198~204쪽, 전체 7쪽
• 주제분류: 의약학 > 기타의약학
• 파일형태: PDF
• 발행일자: 2005.06.30

영문 초록

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 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 alanine, lost the enzymatic activities completely. However, they results suggest that the aspartic acid and glutamic acid at the respective 164th and 200th positions are catalytic residues for enzymatic reaction.

키워드

HFV integrase deletion point mutant