Thermodynamics of cooperative DNA recognition at a replication origin and transcription regulatory site

Binding cooperativity guides the formation of protein-nucleic acid complexes, in particular those that are highly regulated such as replication origins and transcription sites. Using theDNAbinding domain of the origin binding and transcriptional regulator protein E2 from human papillomavirus type 16...

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Autores principales:	Dellarole, M., Sánchez, I.E., De Prat Gay, G.
Formato:	JOUR
Materias:	Cooperativity DNA binding DNA recognition DNA structure Global dynamics Human papillomavirus Isothermal titration calorimetry Protein-nucleic acids Replication origin Strong coupling Transcriptional regulator Binding sites Nucleic acids Proteins Thermodynamics Transcription DNA glycoprotein E2 article beta sheet binding site DNA replication origin DNA transcription enthalpy entropy Human papillomavirus type 11 Human papillomavirus type 18 molecular recognition priority journal protein DNA binding protein domain protein folding thermodynamics Base Sequence Binding Sites DNA-Binding Proteins Human papillomavirus 16 Kinetics Models, Molecular Nucleic Acid Conformation Oncogene Proteins, Viral Protein Binding Protein Structure, Tertiary Regulatory Elements, Transcriptional Replication Origin Transcription, Genetic Human papillomavirus type 16
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_00062960_v49_n48_p10277_Dellarole
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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spelling	todo:paper_00062960_v49_n48_p10277_Dellarole2023-10-03T14:04:31Z Thermodynamics of cooperative DNA recognition at a replication origin and transcription regulatory site Dellarole, M. Sánchez, I.E. De Prat Gay, G. Cooperativity DNA binding DNA recognition DNA structure Global dynamics Human papillomavirus Isothermal titration calorimetry Protein-nucleic acids Replication origin Strong coupling Transcriptional regulator Binding sites Nucleic acids Proteins Thermodynamics Transcription DNA DNA glycoprotein E2 article beta sheet binding site DNA replication origin DNA structure DNA transcription enthalpy entropy Human papillomavirus type 11 Human papillomavirus type 18 molecular recognition priority journal protein DNA binding protein domain protein folding thermodynamics Base Sequence Binding Sites DNA DNA-Binding Proteins Human papillomavirus 16 Kinetics Models, Molecular Nucleic Acid Conformation Oncogene Proteins, Viral Protein Binding Protein Structure, Tertiary Regulatory Elements, Transcriptional Replication Origin Thermodynamics Transcription, Genetic Human papillomavirus type 16 Binding cooperativity guides the formation of protein-nucleic acid complexes, in particular those that are highly regulated such as replication origins and transcription sites. Using theDNAbinding domain of the origin binding and transcriptional regulator protein E2 from human papillomavirus type 16 as model, and through isothermal titration calorimetry analysis, we determined a positive, entropy-driven cooperativity upon binding of the protein to its cognate tandem double E2 site. This cooperativity is associated with a change in DNA structure, where the overall B conformation is maintained. Two homologous E2 domains, those of HPV18 and HPV11, showed that the enthalpic-entropic components of the reaction and DNA deformation can diverge. Because the DNA binding helix is almost identical in the three domains, the differences must lie dispersed throughout this unique dimeric β-barrel fold. This is in surprising agreement with previous results for this domain, which revealed a strong coupling between global dynamics and DNA recognition. © 2010 American Chemical Society. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00062960_v49_n48_p10277_Dellarole
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Cooperativity DNA binding DNA recognition DNA structure Global dynamics Human papillomavirus Isothermal titration calorimetry Protein-nucleic acids Replication origin Strong coupling Transcriptional regulator Binding sites Nucleic acids Proteins Thermodynamics Transcription DNA DNA glycoprotein E2 article beta sheet binding site DNA replication origin DNA structure DNA transcription enthalpy entropy Human papillomavirus type 11 Human papillomavirus type 18 molecular recognition priority journal protein DNA binding protein domain protein folding thermodynamics Base Sequence Binding Sites DNA DNA-Binding Proteins Human papillomavirus 16 Kinetics Models, Molecular Nucleic Acid Conformation Oncogene Proteins, Viral Protein Binding Protein Structure, Tertiary Regulatory Elements, Transcriptional Replication Origin Thermodynamics Transcription, Genetic Human papillomavirus type 16
spellingShingle	Cooperativity DNA binding DNA recognition DNA structure Global dynamics Human papillomavirus Isothermal titration calorimetry Protein-nucleic acids Replication origin Strong coupling Transcriptional regulator Binding sites Nucleic acids Proteins Thermodynamics Transcription DNA DNA glycoprotein E2 article beta sheet binding site DNA replication origin DNA structure DNA transcription enthalpy entropy Human papillomavirus type 11 Human papillomavirus type 18 molecular recognition priority journal protein DNA binding protein domain protein folding thermodynamics Base Sequence Binding Sites DNA DNA-Binding Proteins Human papillomavirus 16 Kinetics Models, Molecular Nucleic Acid Conformation Oncogene Proteins, Viral Protein Binding Protein Structure, Tertiary Regulatory Elements, Transcriptional Replication Origin Thermodynamics Transcription, Genetic Human papillomavirus type 16 Dellarole, M. Sánchez, I.E. De Prat Gay, G. Thermodynamics of cooperative DNA recognition at a replication origin and transcription regulatory site
topic_facet	Cooperativity DNA binding DNA recognition DNA structure Global dynamics Human papillomavirus Isothermal titration calorimetry Protein-nucleic acids Replication origin Strong coupling Transcriptional regulator Binding sites Nucleic acids Proteins Thermodynamics Transcription DNA DNA glycoprotein E2 article beta sheet binding site DNA replication origin DNA structure DNA transcription enthalpy entropy Human papillomavirus type 11 Human papillomavirus type 18 molecular recognition priority journal protein DNA binding protein domain protein folding thermodynamics Base Sequence Binding Sites DNA DNA-Binding Proteins Human papillomavirus 16 Kinetics Models, Molecular Nucleic Acid Conformation Oncogene Proteins, Viral Protein Binding Protein Structure, Tertiary Regulatory Elements, Transcriptional Replication Origin Thermodynamics Transcription, Genetic Human papillomavirus type 16
description	Binding cooperativity guides the formation of protein-nucleic acid complexes, in particular those that are highly regulated such as replication origins and transcription sites. Using theDNAbinding domain of the origin binding and transcriptional regulator protein E2 from human papillomavirus type 16 as model, and through isothermal titration calorimetry analysis, we determined a positive, entropy-driven cooperativity upon binding of the protein to its cognate tandem double E2 site. This cooperativity is associated with a change in DNA structure, where the overall B conformation is maintained. Two homologous E2 domains, those of HPV18 and HPV11, showed that the enthalpic-entropic components of the reaction and DNA deformation can diverge. Because the DNA binding helix is almost identical in the three domains, the differences must lie dispersed throughout this unique dimeric β-barrel fold. This is in surprising agreement with previous results for this domain, which revealed a strong coupling between global dynamics and DNA recognition. © 2010 American Chemical Society.
format	JOUR
author	Dellarole, M. Sánchez, I.E. De Prat Gay, G.
author_facet	Dellarole, M. Sánchez, I.E. De Prat Gay, G.
author_sort	Dellarole, M.
title	Thermodynamics of cooperative DNA recognition at a replication origin and transcription regulatory site
title_short	Thermodynamics of cooperative DNA recognition at a replication origin and transcription regulatory site
title_full	Thermodynamics of cooperative DNA recognition at a replication origin and transcription regulatory site
title_fullStr	Thermodynamics of cooperative DNA recognition at a replication origin and transcription regulatory site
title_full_unstemmed	Thermodynamics of cooperative DNA recognition at a replication origin and transcription regulatory site
title_sort	thermodynamics of cooperative dna recognition at a replication origin and transcription regulatory site
url	http://hdl.handle.net/20.500.12110/paper_00062960_v49_n48_p10277_Dellarole
work_keys_str_mv	AT dellarolem thermodynamicsofcooperativednarecognitionatareplicationoriginandtranscriptionregulatorysite AT sanchezie thermodynamicsofcooperativednarecognitionatareplicationoriginandtranscriptionregulatorysite AT depratgayg thermodynamicsofcooperativednarecognitionatareplicationoriginandtranscriptionregulatorysite
_version_	1782030740002701312

Thermodynamics of cooperative DNA recognition at a replication origin and transcription regulatory site

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