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• W2056515323 endingPage "739" @default.
• W2056515323 startingPage "729" @default.
• W2056515323 abstract "E6 is an oncoprotein implicated in cervical cancers produced by high risk human papillomaviruses. E6 binds specifically to several cellular proteins, including the tumour suppressor p53 and the ubiquitin ligase E6-AP. However, E6 is also a DNA-binding protein which recognizes a structural motive present in four-way junctions. Here, we demonstrate that the C-terminal zinc-binding domain of E6, expressed separately from the rest of the protein, fully retains the selective four-way junction recognition activity. The domain can bind to two identical and independent sites on a single junction, whereas full-length E6 can only bind to one site. The junction bound to either one or two domains adopts an extended square conformation. These results allow us to assign the structure-dependent DNA recognition activity of E6 to its C-terminal domain, which therefore represents a new class of zinc-stabilized DNA-binding module. Comparison with the binding characteristics of other junction-specific proteins enlightens the rules which govern protein-induced deformation of four-way DNA junctions." @default.
• W2056515323 created "2016-06-24" @default.
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• W2056515323 date "2001-01-01" @default.
• W2056515323 modified "2023-09-25" @default.
• W2056515323 title "Specific recognition of four-way DNA junctions by the C-terminal zinc-binding domain of HPV oncoprotein E6" @default.
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• W2056515323 doi "https://doi.org/10.1006/jmbi.2000.4330" @default.
• W2056515323 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11162088" @default.
• W2056515323 hasPublicationYear "2001" @default.
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