The human papillomavirus E7-E2 interaction mechanism in vitro reveals a finely tuned system for modulating available E7 and E2 proteins
Transcription of the human papillomavirus E7 oncoprotein is negatively controlled by the viral E2 protein, and loss of this repression leads to irreversible transformation and carcinogenesis. Here we show that interaction of the HPV16 E7 protein with the DNA binding domain of the E2 protein (E2C) le...
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2009
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| 001 | PAPER-8215 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518203802.0 | ||
| 008 | 190411s2009 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-72449169953 | |
| 024 | 7 | |2 cas |a DNA-Binding Proteins; E2 protein, Human papillomavirus type 16; Oncogene Proteins, Viral; oncogene protein E7, Human papillomavirus type 16; ras Proteins, 3.6.5.2 | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a BICHA | ||
| 100 | 1 | |a Smal, C. | |
| 245 | 1 | 4 | |a The human papillomavirus E7-E2 interaction mechanism in vitro reveals a finely tuned system for modulating available E7 and E2 proteins |
| 260 | |c 2009 | ||
| 270 | 1 | 0 | |m De Prat-Gay, G.; Fundación Instituto Leloir, Instituto de Investigaciones Bioquímicas, CONICET, Patricias Argentinas 435, 1405 Buenos Aires, Argentina; email: gpg@leloir.org.ar |
| 506 | |2 openaire |e Política editorial | ||
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| 520 | 3 | |a Transcription of the human papillomavirus E7 oncoprotein is negatively controlled by the viral E2 protein, and loss of this repression leads to irreversible transformation and carcinogenesis. Here we show that interaction of the HPV16 E7 protein with the DNA binding domain of the E2 protein (E2C) leads to ionic strength-dependent hetero-oligomerization even at the lowest concentrations measurable. Titration experiments followed by light scattering and native gel electrophoresis show insoluble oligomeric complexes with a ≥2000 nm diameter and intermediate soluble complexes 40 and 115 nm in diameter, respectively, formed in excess of E2C. Adiscrete oligomeric soluble complex formed in excess of E7 displays a diameter of 12 nm. The N-terminal domain of E7 interacts with E2C with a KD of 0.1 μM, where the stretch of residues 25-40 of E7, encompassing both a PEST motif and phosphorylation sites, is sufficient for the interaction. Displacement of the soluble E7-E2C complex by an E2 site DNA duplex and site-directed mutagenesis indicate that the protein-protein interface involves the DNA binding helix of E2. The formation of complexes of different sizes and properties in excess of either of the viral proteins reveals a finely tuned mechanism that could regulate the intracellular levels of both proteins as infection and transformation progress. Sequestering E2 into E7-E2 oligomers provides a possible additional route to uncontrolled E7 expression, in addition and prior to the disruption of the E2 gene during viral integration into the host genome. © 2009 American Chemical Society. |l eng | |
| 593 | |a Fundación Instituto Leloir, Instituto de Investigaciones Bioquímicas, CONICET, Patricias Argentinas 435, 1405 Buenos Aires, Argentina | ||
| 593 | |a Facultad de Ciencias Exactas Y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina | ||
| 593 | |a Department of Biochemistry, School of Medical Sciences, University of Bristol, Bristol BS8 1TD, United Kingdom | ||
| 593 | |a Medical Research Council, Centre for Protein Engineering, Cambridge CB2 0QH, United Kingdom | ||
| 690 | 1 | 0 | |a DIFFERENT SIZES |
| 690 | 1 | 0 | |a DNA BINDING |
| 690 | 1 | 0 | |a DNA BINDING DOMAIN |
| 690 | 1 | 0 | |a DNA DUPLEXES |
| 690 | 1 | 0 | |a E7 ONCOPROTEIN |
| 690 | 1 | 0 | |a GEL ELECTROPHORESIS |
| 690 | 1 | 0 | |a HETERO-OLIGOMERIZATION |
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| 690 | 1 | 0 | |a PHOSPHORYLATION SITES |
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| 690 | 1 | 0 | |a SITE DIRECTED MUTAGENESIS |
| 690 | 1 | 0 | |a SOLUBLE COMPLEXES |
| 690 | 1 | 0 | |a VIRAL PROTEINS |
| 690 | 1 | 0 | |a BINDING SITES |
| 690 | 1 | 0 | |a COMPLEXATION |
| 690 | 1 | 0 | |a DNA |
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| 690 | 1 | 0 | |a ENZYME ACTIVITY |
| 690 | 1 | 0 | |a IONIC STRENGTH |
| 690 | 1 | 0 | |a NUCLEIC ACIDS |
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| 690 | 1 | 0 | |a OLIGOMERS |
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| 690 | 1 | 0 | |a PROTEIN E7 |
| 690 | 1 | 0 | |a PROTEIN VP2 |
| 690 | 1 | 0 | |a AMINO TERMINAL SEQUENCE |
| 690 | 1 | 0 | |a ARTICLE |
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| 690 | 1 | 0 | |a PRIORITY JOURNAL |
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| 690 | 1 | 0 | |a CELL LINE, TUMOR |
| 690 | 1 | 0 | |a CELL PROLIFERATION |
| 690 | 1 | 0 | |a DNA-BINDING PROTEINS |
| 690 | 1 | 0 | |a HUMAN PAPILLOMAVIRUS 16 |
| 690 | 1 | 0 | |a HUMANS |
| 690 | 1 | 0 | |a MOLECULAR SEQUENCE DATA |
| 690 | 1 | 0 | |a ONCOGENE PROTEINS, VIRAL |
| 690 | 1 | 0 | |a PROTEIN STRUCTURE, TERTIARY |
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| 700 | 1 | |a Wetzler, D.E. | |
| 700 | 1 | |a Dantur, K.I. | |
| 700 | 1 | |a Chemes, L.B. | |
| 700 | 1 | |a Garcia-Alai, M.M. | |
| 700 | 1 | |a Dellarole, M. | |
| 700 | 1 | |a Alonso, L.G. | |
| 700 | 1 | |a Gaston, K. | |
| 700 | 1 | |a De Prat-Gay, G. | |
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