Characterization of the minimal DNA binding domain of the human papillomavirus e1 helicase: fluorescence anisotropy studies and characterization of a dimerization-defective mutant protein.

Abstract excerpt

The E1 helicase of papillomaviruses is required for replication of the viral double-stranded DNA genome, in conjunction with cellular factors. DNA replication is initiated at the viral origin by the assembly of E1 monomers into oligomeric complexes that have unwinding activity. In vivo, this process is catalyzed by the viral E2 protein, which recruits E1 specifically at the origin. For bovine papillomavirus (BPV)...

Topics

• Base Sequence
• DNA Helicases
• DNA, Viral
• DNA-Binding Proteins
• Dimerization
• Fluorescence Polarization
• Humans
• Molecular Sequence Data
• Mutation
• Papillomaviridae
• Viral Proteins