A novel DNA binding and nuclease activity in domain III of Mu transposase: evidence for a catalytic region involved in donor cleavage.

Abstract excerpt

The Mu A protein is a 75 kDa transposase organized into three structural domains. By severing the C-terminal region (domain III) from the remainder of the protein, we unmasked a novel non-specific DNA binding and nuclease activity in this region. Deletion analysis localized both activities to a 26 amino acid stretch (aa 575-600) which remarkably remained active in DNA binding and cleavage. The two activities were...

Topics

• Amino Acid Sequence
• Bacteriophage mu
• Base Sequence
• Binding Sites
• Catalysis
• DNA, Viral
• DNA-Binding Proteins
• Endodeoxyribonucleases
• Enhancer Elements, Genetic
• Molecular Sequence Data
• Mutation