A strained DNA binding helix is conserved for site recognition, folding nucleation, and conformational modulation

Autores
Wetzler, Diana Elena; Gallo, Mariana; Melis, Riccardo; Eliseo, Tomasso; Nadra, Alejandro Daniel; Ferreiro, Diego; Paci, Maurizio; Sánchez Miguel, Ignacio Enrique; Cicero, Daniel Oscar; de Prat Gay, Gonzalo
Año de publicación
2009
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Nucleic acid recognition is often mediated by alpha-helices or disordered regions that fold into alpha-helix on binding. A peptide bearing the DNA recognition helix of HPV16 E2 displays type II polyproline (PII) structure as judged by pH, temperature, and solvent effects on the CD spectra. NMR experiments indicate that the canonical alpha-helix is stabilized at the N-terminus, while the PII forms at the C-terminus half of the peptide. Re-examination of the dihedral angles of the DNA binding helix in the crystal structure and analysis of the NMR chemical shift indexes confirm that the N-terminus half is a canonical alpha-helix, while the C-terminal half adopts a 3(10) helix structure. These regions precisely match two locally driven folding nucleii, which partake in the native hydrophobic core and modulate a conformational switch in the DNA binding helix. The peptide shows only weak and unspecific residual DNA binding, 10(4)-fold lower affinity, and 500-fold lower discrimination capacity compared with the domain. Thus, the precise side chain conformation required for modulated and tight physiological binding by HPV E2 is largely determined by the noncanonical strained alpha-helix conformation, "presented" by this unique architecture.
Fil: Wetzler, Diana Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Gallo, Mariana. Universita Tor Vergata; Italia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Melis, Riccardo. Universita Tor Vergata; Italia
Fil: Eliseo, Tomasso. Universita Tor Vergata; Italia
Fil: Nadra, Alejandro Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. Universita Tor Vergata; Italia. Centro de Regulación Genómica; España
Fil: Ferreiro, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Paci, Maurizio. Universita Tor Vergata; Italia
Fil: Sánchez Miguel, Ignacio Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Cicero, Daniel Oscar. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universita Tor Vergata; Italia
Fil: de Prat Gay, Gonzalo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Materia
PROTEIN-DNA
AMYLOID
E2
HPV
FOLDING
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/25935
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/25935
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling A strained DNA binding helix is conserved for site recognition, folding nucleation, and conformational modulationWetzler, Diana ElenaGallo, MarianaMelis, RiccardoEliseo, TomassoNadra, Alejandro DanielFerreiro, DiegoPaci, MaurizioSánchez Miguel, Ignacio EnriqueCicero, Daniel Oscarde Prat Gay, GonzaloPROTEIN-DNAAMYLOIDE2HPVFOLDINGhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Nucleic acid recognition is often mediated by alpha-helices or disordered regions that fold into alpha-helix on binding. A peptide bearing the DNA recognition helix of HPV16 E2 displays type II polyproline (PII) structure as judged by pH, temperature, and solvent effects on the CD spectra. NMR experiments indicate that the canonical alpha-helix is stabilized at the N-terminus, while the PII forms at the C-terminus half of the peptide. Re-examination of the dihedral angles of the DNA binding helix in the crystal structure and analysis of the NMR chemical shift indexes confirm that the N-terminus half is a canonical alpha-helix, while the C-terminal half adopts a 3(10) helix structure. These regions precisely match two locally driven folding nucleii, which partake in the native hydrophobic core and modulate a conformational switch in the DNA binding helix. The peptide shows only weak and unspecific residual DNA binding, 10(4)-fold lower affinity, and 500-fold lower discrimination capacity compared with the domain. Thus, the precise side chain conformation required for modulated and tight physiological binding by HPV E2 is largely determined by the noncanonical strained alpha-helix conformation, "presented" by this unique architecture.Fil: Wetzler, Diana Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Gallo, Mariana. Universita Tor Vergata; Italia. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Melis, Riccardo. Universita Tor Vergata; ItaliaFil: Eliseo, Tomasso. Universita Tor Vergata; ItaliaFil: Nadra, Alejandro Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. Universita Tor Vergata; Italia. Centro de Regulación Genómica; EspañaFil: Ferreiro, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Paci, Maurizio. Universita Tor Vergata; ItaliaFil: Sánchez Miguel, Ignacio Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Cicero, Daniel Oscar. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universita Tor Vergata; ItaliaFil: de Prat Gay, Gonzalo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaJohn Wiley & Sons Inc2009-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/25935Wetzler, Diana Elena; Gallo, Mariana; Melis, Riccardo; Eliseo, Tomasso; Nadra, Alejandro Daniel; et al.; A strained DNA binding helix is conserved for site recognition, folding nucleation, and conformational modulation; John Wiley & Sons Inc; Biopolymers; 91; 6; 6-2009; 432-4430006-35251097-0282CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/bip.21146info:eu-repo/semantics/altIdentifier/doi/10.1002/bip.21146info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:59:10Zoai:ri.conicet.gov.ar:11336/25935instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 09:59:11.227CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A strained DNA binding helix is conserved for site recognition, folding nucleation, and conformational modulation
title A strained DNA binding helix is conserved for site recognition, folding nucleation, and conformational modulation
spellingShingle A strained DNA binding helix is conserved for site recognition, folding nucleation, and conformational modulation
Wetzler, Diana Elena
PROTEIN-DNA
AMYLOID
E2
HPV
FOLDING
title_short A strained DNA binding helix is conserved for site recognition, folding nucleation, and conformational modulation
title_full A strained DNA binding helix is conserved for site recognition, folding nucleation, and conformational modulation
title_fullStr A strained DNA binding helix is conserved for site recognition, folding nucleation, and conformational modulation
title_full_unstemmed A strained DNA binding helix is conserved for site recognition, folding nucleation, and conformational modulation
title_sort A strained DNA binding helix is conserved for site recognition, folding nucleation, and conformational modulation
dc.creator.none.fl_str_mv Wetzler, Diana Elena
Gallo, Mariana
Melis, Riccardo
Eliseo, Tomasso
Nadra, Alejandro Daniel
Ferreiro, Diego
Paci, Maurizio
Sánchez Miguel, Ignacio Enrique
Cicero, Daniel Oscar
de Prat Gay, Gonzalo
author Wetzler, Diana Elena
author_facet Wetzler, Diana Elena
Gallo, Mariana
Melis, Riccardo
Eliseo, Tomasso
Nadra, Alejandro Daniel
Ferreiro, Diego
Paci, Maurizio
Sánchez Miguel, Ignacio Enrique
Cicero, Daniel Oscar
de Prat Gay, Gonzalo
author_role author
author2 Gallo, Mariana
Melis, Riccardo
Eliseo, Tomasso
Nadra, Alejandro Daniel
Ferreiro, Diego
Paci, Maurizio
Sánchez Miguel, Ignacio Enrique
Cicero, Daniel Oscar
de Prat Gay, Gonzalo
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv PROTEIN-DNA
AMYLOID
E2
HPV
FOLDING
topic PROTEIN-DNA
AMYLOID
E2
HPV
FOLDING
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Nucleic acid recognition is often mediated by alpha-helices or disordered regions that fold into alpha-helix on binding. A peptide bearing the DNA recognition helix of HPV16 E2 displays type II polyproline (PII) structure as judged by pH, temperature, and solvent effects on the CD spectra. NMR experiments indicate that the canonical alpha-helix is stabilized at the N-terminus, while the PII forms at the C-terminus half of the peptide. Re-examination of the dihedral angles of the DNA binding helix in the crystal structure and analysis of the NMR chemical shift indexes confirm that the N-terminus half is a canonical alpha-helix, while the C-terminal half adopts a 3(10) helix structure. These regions precisely match two locally driven folding nucleii, which partake in the native hydrophobic core and modulate a conformational switch in the DNA binding helix. The peptide shows only weak and unspecific residual DNA binding, 10(4)-fold lower affinity, and 500-fold lower discrimination capacity compared with the domain. Thus, the precise side chain conformation required for modulated and tight physiological binding by HPV E2 is largely determined by the noncanonical strained alpha-helix conformation, "presented" by this unique architecture.
Fil: Wetzler, Diana Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Gallo, Mariana. Universita Tor Vergata; Italia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Melis, Riccardo. Universita Tor Vergata; Italia
Fil: Eliseo, Tomasso. Universita Tor Vergata; Italia
Fil: Nadra, Alejandro Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. Universita Tor Vergata; Italia. Centro de Regulación Genómica; España
Fil: Ferreiro, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Paci, Maurizio. Universita Tor Vergata; Italia
Fil: Sánchez Miguel, Ignacio Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Cicero, Daniel Oscar. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universita Tor Vergata; Italia
Fil: de Prat Gay, Gonzalo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
description Nucleic acid recognition is often mediated by alpha-helices or disordered regions that fold into alpha-helix on binding. A peptide bearing the DNA recognition helix of HPV16 E2 displays type II polyproline (PII) structure as judged by pH, temperature, and solvent effects on the CD spectra. NMR experiments indicate that the canonical alpha-helix is stabilized at the N-terminus, while the PII forms at the C-terminus half of the peptide. Re-examination of the dihedral angles of the DNA binding helix in the crystal structure and analysis of the NMR chemical shift indexes confirm that the N-terminus half is a canonical alpha-helix, while the C-terminal half adopts a 3(10) helix structure. These regions precisely match two locally driven folding nucleii, which partake in the native hydrophobic core and modulate a conformational switch in the DNA binding helix. The peptide shows only weak and unspecific residual DNA binding, 10(4)-fold lower affinity, and 500-fold lower discrimination capacity compared with the domain. Thus, the precise side chain conformation required for modulated and tight physiological binding by HPV E2 is largely determined by the noncanonical strained alpha-helix conformation, "presented" by this unique architecture.
publishDate 2009
dc.date.none.fl_str_mv 2009-06
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/25935
Wetzler, Diana Elena; Gallo, Mariana; Melis, Riccardo; Eliseo, Tomasso; Nadra, Alejandro Daniel; et al.; A strained DNA binding helix is conserved for site recognition, folding nucleation, and conformational modulation; John Wiley & Sons Inc; Biopolymers; 91; 6; 6-2009; 432-443
0006-3525
1097-0282
CONICET Digital
CONICET
url http://hdl.handle.net/11336/25935
identifier_str_mv Wetzler, Diana Elena; Gallo, Mariana; Melis, Riccardo; Eliseo, Tomasso; Nadra, Alejandro Daniel; et al.; A strained DNA binding helix is conserved for site recognition, folding nucleation, and conformational modulation; John Wiley & Sons Inc; Biopolymers; 91; 6; 6-2009; 432-443
0006-3525
1097-0282
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/bip.21146
info:eu-repo/semantics/altIdentifier/doi/10.1002/bip.21146
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv John Wiley & Sons Inc
publisher.none.fl_str_mv John Wiley & Sons Inc
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.13397

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