| Title | Site-specific Mutagenesis에 의한 PRD1 DNA polymerase의 활성부위 결정 | ||
| Author | 황정원 · 정구홍 | ||
| Address | 서울대학교 사범대학 생물교육학과 | ||
| Bibliography | Korean Journal of Microbiology, 29(4),209-214, 1991 | ||
| DOI | |||
| Key Words | DNA Polymerase, Structure-Function Analysis, Conserved Amino Acid | ||
| Abstract | The PRD1 DNA polymerase is a small multi-functional enzyme containing conserved amino acid sequences shared by family B DNA polymerases. Thus the PRD1 DNA polymerase provides an useful model system with which to study structure-functional relationships of DNA polymerase molecules. In order to investigate the functional and structural roles of the highly conserved amino acid sequences, we have introduced three mutations into a conserved amino acid of the PRD1 DNA polymerase. Genetic complementation study indicated that each mutation inactivated DNA polymerase catalytic activity. | ||
| Download PDF | Kor_290402_209-214p.pdf | ||