| Title | An Analysis of the Arm-type Site Binding Domain of Bacteriophage γ Integrase |
|---|---|
| Author | Cho, Eun Hee |
| Address | Department of Science Deucation, College of Education, Chosun University, Kwangju |
| Bibliography | Journal of Microbiology, 33(2),165-170, 1995, |
| DOI | |
| Key Words | bacteriophage γ, integrase, sequence-specific DNA binding, functional somain of protein |
| Abstract | The 356 amino acid long lambda integrase protein of bacteriophage λ constains two autonomous DNA binding domains with distinct sequence specificities. The amino terminal domain of integrase is implicated to bind to the arm-type sequences and the carboxyl domain interacts with the coretype sequencess. As a first step to understand the molecular mechanism of the integrase-DNA interaction at the arm-type site, the int(am)94 gene carrying an amber mutation at the 94th codon of the int was cloned under the control of the P_tac promoter and the lacI^q gene. The Int(am)94 mutant protein of amino terminal 93 amino acid residues can be produced at high level from a suppressor free strain harboring the plasmid pInt(am)94. The arm-type binding activity of Int(am)94 were measured in vivo and in vitro. A comparison of the arm-type binding properties of the wild-type integrase and the truncated Int(am)94 mutant indicated that the truncated fragment containing 93 amino acid residues carry all the determinants for DNA binding at the arm-type sites. |
| Download PDF | Eng_330215_165-170p.pdf |