A protein-DNA binding mechanism proceeds through multi-state or two-state parallel pathways
The DNA-binding mechanism of the dimeric C-terminal domain of the papillomavirus E2 protein with its specific DNA target was investigated and shown to proceed through two parallel pathways. A sequential multi-step reaction is initiated by the diffusion-controlled formation of an encounter complex, w...
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2003
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00222836_v331_n1_p89_Ferreiro http://hdl.handle.net/20.500.12110/paper_00222836_v331_n1_p89_Ferreiro |
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paper:paper_00222836_v331_n1_p89_Ferreiro2023-06-08T14:48:43Z A protein-DNA binding mechanism proceeds through multi-state or two-state parallel pathways Ferreiro, Diego U. de Prat Gay, Gonzalo DNA-binding HPV-E2 Protein-DNA Recognition Stopped-flow DNA base virus protein article DNA binding nucleotide sequence Papilloma virus priority journal protein analysis protein DNA binding protein domain Papillomavirus The DNA-binding mechanism of the dimeric C-terminal domain of the papillomavirus E2 protein with its specific DNA target was investigated and shown to proceed through two parallel pathways. A sequential multi-step reaction is initiated by the diffusion-controlled formation of an encounter complex, with no evidence of base sequence discrimination capacity. Following a substantial conformational rearrangement of the protein, a solvent exclusion step leading to the formation of a final protein-DNA complex was identified. This last step involves the largest burial of surface area from the interface and involves the consolidation of the direct readout of the DNA bases. Double-jump stopped-flow experiments allowed us to characterize the sequence of events and demonstrated that a fast-formed consolidated complex can take place through a parallel route. We present the simplest model for the overall mechanism with a description of all the intermediate species in energetic terms. © 2003 Elsevier Ltd. All rights reserved. Fil:Ferreiro, D.U. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:De Prat-Gay, G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2003 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00222836_v331_n1_p89_Ferreiro http://hdl.handle.net/20.500.12110/paper_00222836_v331_n1_p89_Ferreiro |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
DNA-binding HPV-E2 Protein-DNA Recognition Stopped-flow DNA base virus protein article DNA binding nucleotide sequence Papilloma virus priority journal protein analysis protein DNA binding protein domain Papillomavirus |
| spellingShingle |
DNA-binding HPV-E2 Protein-DNA Recognition Stopped-flow DNA base virus protein article DNA binding nucleotide sequence Papilloma virus priority journal protein analysis protein DNA binding protein domain Papillomavirus Ferreiro, Diego U. de Prat Gay, Gonzalo A protein-DNA binding mechanism proceeds through multi-state or two-state parallel pathways |
| topic_facet |
DNA-binding HPV-E2 Protein-DNA Recognition Stopped-flow DNA base virus protein article DNA binding nucleotide sequence Papilloma virus priority journal protein analysis protein DNA binding protein domain Papillomavirus |
| description |
The DNA-binding mechanism of the dimeric C-terminal domain of the papillomavirus E2 protein with its specific DNA target was investigated and shown to proceed through two parallel pathways. A sequential multi-step reaction is initiated by the diffusion-controlled formation of an encounter complex, with no evidence of base sequence discrimination capacity. Following a substantial conformational rearrangement of the protein, a solvent exclusion step leading to the formation of a final protein-DNA complex was identified. This last step involves the largest burial of surface area from the interface and involves the consolidation of the direct readout of the DNA bases. Double-jump stopped-flow experiments allowed us to characterize the sequence of events and demonstrated that a fast-formed consolidated complex can take place through a parallel route. We present the simplest model for the overall mechanism with a description of all the intermediate species in energetic terms. © 2003 Elsevier Ltd. All rights reserved. |
| author |
Ferreiro, Diego U. de Prat Gay, Gonzalo |
| author_facet |
Ferreiro, Diego U. de Prat Gay, Gonzalo |
| author_sort |
Ferreiro, Diego U. |
| title |
A protein-DNA binding mechanism proceeds through multi-state or two-state parallel pathways |
| title_short |
A protein-DNA binding mechanism proceeds through multi-state or two-state parallel pathways |
| title_full |
A protein-DNA binding mechanism proceeds through multi-state or two-state parallel pathways |
| title_fullStr |
A protein-DNA binding mechanism proceeds through multi-state or two-state parallel pathways |
| title_full_unstemmed |
A protein-DNA binding mechanism proceeds through multi-state or two-state parallel pathways |
| title_sort |
protein-dna binding mechanism proceeds through multi-state or two-state parallel pathways |
| publishDate |
2003 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00222836_v331_n1_p89_Ferreiro http://hdl.handle.net/20.500.12110/paper_00222836_v331_n1_p89_Ferreiro |
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1768542350717485056 |