A protein-DNA binding mechanism proceeds through multi-state or two-state parallel pathways

Mostrar todas las versiones(2)

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...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Ferreiro, D.U., De Prat-Gay, G.
Formato: JOUR
Materias:
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
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00222836_v331_n1_p89_Ferreiro
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id todo:paper_00222836_v331_n1_p89_Ferreiro
record_format dspace
spelling todo:paper_00222836_v331_n1_p89_Ferreiro2023-10-03T14:30:21Z A protein-DNA binding mechanism proceeds through multi-state or two-state parallel pathways Ferreiro, D.U. De Prat-Gay, G. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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, D.U.
De Prat-Gay, G.
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.
format JOUR
author Ferreiro, D.U.
De Prat-Gay, G.
author_facet Ferreiro, D.U.
De Prat-Gay, G.
author_sort Ferreiro, D.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
url http://hdl.handle.net/20.500.12110/paper_00222836_v331_n1_p89_Ferreiro
work_keys_str_mv AT ferreirodu aproteindnabindingmechanismproceedsthroughmultistateortwostateparallelpathways
AT depratgayg aproteindnabindingmechanismproceedsthroughmultistateortwostateparallelpathways
AT ferreirodu proteindnabindingmechanismproceedsthroughmultistateortwostateparallelpathways
AT depratgayg proteindnabindingmechanismproceedsthroughmultistateortwostateparallelpathways
_version_ 1807316061596418048

Ejemplares similares