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Domain substructure of HPV E6 oncoprotein: biophysical characterization of the E6 C-terminal DNA-binding domain

MPG-Autoren
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Stier,  Gunter
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

Externe Ressourcen

http://pubs.acs.org/doi/pdf/10.1021/bi026980c
(beliebiger Volltext)

https://doi.org/10.1021/bi026980c
(beliebiger Volltext)

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Zitation

Nominé, Y., Charbonnier, S., Ristriani, T., Stier, G., Masson, M., Cavusoglu, N., et al. (2003). Domain substructure of HPV E6 oncoprotein: biophysical characterization of the E6 C-terminal DNA-binding domain. Biochemistry, 42(17), 4909-4917. doi:10.1021/bi026980c.


Zitierlink: https://hdl.handle.net/21.11116/0000-0000-3C91-9
Zusammenfassung
E6 is a viral oncoprotein implicated in cervical cancers, produced by high-risk human papillomaviruses (HPVs). Structural data concerning this protein are scarce due to the difficulty of producing recombinant E6. Recently, we described the expression and purification of a stable, folded, and biologically active HPV16 E6 mutant called E6 6C/6S. Here, we analyzed the domain substructure of this mutated E6. Nonspecific proteolysis of full-length E6 6C/6S (158 residues) yielded N-terminal and C-terminal fragments encompassing residues 7-83 and 87-158, respectively. The C-terminal fragment of residues 87-158 was cloned, overexpressed, and purified at concentrations as high as 1 mM. The purified domain retains the selective four-way DNA junction recognition activity of the full-length E6 protein. Using UV absorption, UV fluorescence, circular dichroism, and nuclear magnetic resonance, we show that the peptide is primarily monomeric and folded with equal proportions of alpha-helix and beta-sheet secondary structure.