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KMID : 0624620090420030160
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BMB Reports
2009 Volume.42 No. 3 p.160 ~ p.165
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Moderately thermostable phage Φ11 Cro repressor has novel DNA-binding capacity and physicochemical properties
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Das Malabika
Ganguly Tridib
Bandhu Amitava
Mondal Rajkrishna
Chanda Palas Kumar
Jana Biswanath
Sau Subrata
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Abstract
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The temperate Staphylococcus aureus phage Φ11 harbors cI and cro repressor genes similar to those of lambdoid phages. Using extremely pure Φ11 Cro (the product of the Φ11 cro gene) we demonstrated that this protein possesses a single domain structure, forms dimers in solution at micromolar concentrations and maintains a largely α-helical structure even at 45oC. Φ11 Cro was sensitive to thermolysin at temperatures ranging from 55-75oC and began to aggregate at ~63oC, suggesting that the protein is moderately thermostable. Of the three homologous 15-bp operators (O1, O2, and O3) in the Φ11 cI-cro intergenic region, Φ11 Cro only binds efficiently to O3, which is located upstream of the cI gene. Our comparative analyses indicate that the DNA binding capacity, secondary structure and dimerization efficiency of thermostable Φ11 Cro are distinct from those of P22 Cro and λ Cro, the best characterized representatives of the two structurally different Cro families.
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KEYWORD
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Cro, Dimer, Operator, Single domain, Φ11
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