Frataxin from Psychromonas ingrahamii as a model to study stability modulation within the CyaY protein family

Autores
Roman, Ernesto Andres; Faraj, Santiago Enrique; Cousido Siah, Alexandra; Mitschler, André; Podjarny, Alberto Daniel; Santos, Javier
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Adaptation of life to low temperatures influences both protein stability and flexibility. Thus, proteins from psychrophilic organisms are excellent models to study relations between these properties. Here we focused on frataxin from Psychromonas ingrahamii (pFXN), an extreme psychrophilic sea ice bacterium that can grow at temperatures as low as - 12 C. This α/β protein is highly conserved and plays a key role in iron homeostasis as an iron chaperone. In contrast to other frataxin homologs, chemical and temperature unfolding experiments showed that the thermodynamic stability of pFXN is strongly modulated by pHs: Ranging from 5.5 ± 0.9 (pH 6.0) to 0.9 ± 0.3 kcal mol- 1 (pH 8.0). This protein was crystallized and its X-ray structure solved at 1.45 Å. Comparison of B-factor profiles between Escherichia coli and P. ingrahamii frataxin variants (51% of identity) suggests that, although both proteins share the same structural features, their flexibility distribution is different. Molecular dynamics simulations showed that protonation of His44 or His67 in pFXN lowers the mobility of regions encompassing residues 20-30 and the C-terminal end, probably through favorable electrostatic interactions with residues Asp27, Glu42 and Glu99. Since the C-terminal end of the protein is critical for the stabilization of the frataxin fold, the predictions presented may be reporting on the microscopic origin of the decrease in global stability produced near neutral pH in the psychrophilic variant. We propose that suboptimal electrostatic interactions may have been an evolutionary strategy for the adaptation of frataxin flexibility and function to cold environments.
Fil: Roman, Ernesto Andres. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Faraj, Santiago Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Cousido Siah, Alexandra. Université de Strasbourg; Francia
Fil: Mitschler, André. Université de Strasbourg; Francia
Fil: Podjarny, Alberto Daniel. Université de Strasbourg; Francia
Fil: Santos, Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Materia
CRYSTALLOGRAPHY
MOLECULAR DYNAMICS SIMULATIONS
PROTEIN DYNAMICS
PROTEIN FLEXIBILITY
PROTEIN STABILITY
STABILITY MODULATION
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/84739
Acceder
id CONICETDig_ed7ad51833ca53e7ebdb179433d50100
oai_identifier_str oai:ri.conicet.gov.ar:11336/84739
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Frataxin from Psychromonas ingrahamii as a model to study stability modulation within the CyaY protein familyRoman, Ernesto AndresFaraj, Santiago EnriqueCousido Siah, AlexandraMitschler, AndréPodjarny, Alberto DanielSantos, JavierCRYSTALLOGRAPHYMOLECULAR DYNAMICS SIMULATIONSPROTEIN DYNAMICSPROTEIN FLEXIBILITYPROTEIN STABILITYSTABILITY MODULATIONhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Adaptation of life to low temperatures influences both protein stability and flexibility. Thus, proteins from psychrophilic organisms are excellent models to study relations between these properties. Here we focused on frataxin from Psychromonas ingrahamii (pFXN), an extreme psychrophilic sea ice bacterium that can grow at temperatures as low as - 12 C. This α/β protein is highly conserved and plays a key role in iron homeostasis as an iron chaperone. In contrast to other frataxin homologs, chemical and temperature unfolding experiments showed that the thermodynamic stability of pFXN is strongly modulated by pHs: Ranging from 5.5 ± 0.9 (pH 6.0) to 0.9 ± 0.3 kcal mol- 1 (pH 8.0). This protein was crystallized and its X-ray structure solved at 1.45 Å. Comparison of B-factor profiles between Escherichia coli and P. ingrahamii frataxin variants (51% of identity) suggests that, although both proteins share the same structural features, their flexibility distribution is different. Molecular dynamics simulations showed that protonation of His44 or His67 in pFXN lowers the mobility of regions encompassing residues 20-30 and the C-terminal end, probably through favorable electrostatic interactions with residues Asp27, Glu42 and Glu99. Since the C-terminal end of the protein is critical for the stabilization of the frataxin fold, the predictions presented may be reporting on the microscopic origin of the decrease in global stability produced near neutral pH in the psychrophilic variant. We propose that suboptimal electrostatic interactions may have been an evolutionary strategy for the adaptation of frataxin flexibility and function to cold environments.Fil: Roman, Ernesto Andres. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; ArgentinaFil: Faraj, Santiago Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; ArgentinaFil: Cousido Siah, Alexandra. Université de Strasbourg; FranciaFil: Mitschler, André. Université de Strasbourg; FranciaFil: Podjarny, Alberto Daniel. Université de Strasbourg; FranciaFil: Santos, Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; ArgentinaElsevier Science2013-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/84739Roman, Ernesto Andres; Faraj, Santiago Enrique; Cousido Siah, Alexandra; Mitschler, André; Podjarny, Alberto Daniel; et al.; Frataxin from Psychromonas ingrahamii as a model to study stability modulation within the CyaY protein family; Elsevier Science; Biochimica Et Biophysica Acta-proteins And Proteomics; 1834; 6; 6-2013; 1168-11801570-9639CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1570963913000782info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbapap.2013.02.015info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:17:18Zoai:ri.conicet.gov.ar:11336/84739instacron: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:34982025-10-15 15:17:18.329CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Frataxin from Psychromonas ingrahamii as a model to study stability modulation within the CyaY protein family
title Frataxin from Psychromonas ingrahamii as a model to study stability modulation within the CyaY protein family
spellingShingle Frataxin from Psychromonas ingrahamii as a model to study stability modulation within the CyaY protein family
Roman, Ernesto Andres
CRYSTALLOGRAPHY
MOLECULAR DYNAMICS SIMULATIONS
PROTEIN DYNAMICS
PROTEIN FLEXIBILITY
PROTEIN STABILITY
STABILITY MODULATION
title_short Frataxin from Psychromonas ingrahamii as a model to study stability modulation within the CyaY protein family
title_full Frataxin from Psychromonas ingrahamii as a model to study stability modulation within the CyaY protein family
title_fullStr Frataxin from Psychromonas ingrahamii as a model to study stability modulation within the CyaY protein family
title_full_unstemmed Frataxin from Psychromonas ingrahamii as a model to study stability modulation within the CyaY protein family
title_sort Frataxin from Psychromonas ingrahamii as a model to study stability modulation within the CyaY protein family
dc.creator.none.fl_str_mv Roman, Ernesto Andres
Faraj, Santiago Enrique
Cousido Siah, Alexandra
Mitschler, André
Podjarny, Alberto Daniel
Santos, Javier
author Roman, Ernesto Andres
author_facet Roman, Ernesto Andres
Faraj, Santiago Enrique
Cousido Siah, Alexandra
Mitschler, André
Podjarny, Alberto Daniel
Santos, Javier
author_role author
author2 Faraj, Santiago Enrique
Cousido Siah, Alexandra
Mitschler, André
Podjarny, Alberto Daniel
Santos, Javier
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv CRYSTALLOGRAPHY
MOLECULAR DYNAMICS SIMULATIONS
PROTEIN DYNAMICS
PROTEIN FLEXIBILITY
PROTEIN STABILITY
STABILITY MODULATION
topic CRYSTALLOGRAPHY
MOLECULAR DYNAMICS SIMULATIONS
PROTEIN DYNAMICS
PROTEIN FLEXIBILITY
PROTEIN STABILITY
STABILITY MODULATION
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Adaptation of life to low temperatures influences both protein stability and flexibility. Thus, proteins from psychrophilic organisms are excellent models to study relations between these properties. Here we focused on frataxin from Psychromonas ingrahamii (pFXN), an extreme psychrophilic sea ice bacterium that can grow at temperatures as low as - 12 C. This α/β protein is highly conserved and plays a key role in iron homeostasis as an iron chaperone. In contrast to other frataxin homologs, chemical and temperature unfolding experiments showed that the thermodynamic stability of pFXN is strongly modulated by pHs: Ranging from 5.5 ± 0.9 (pH 6.0) to 0.9 ± 0.3 kcal mol- 1 (pH 8.0). This protein was crystallized and its X-ray structure solved at 1.45 Å. Comparison of B-factor profiles between Escherichia coli and P. ingrahamii frataxin variants (51% of identity) suggests that, although both proteins share the same structural features, their flexibility distribution is different. Molecular dynamics simulations showed that protonation of His44 or His67 in pFXN lowers the mobility of regions encompassing residues 20-30 and the C-terminal end, probably through favorable electrostatic interactions with residues Asp27, Glu42 and Glu99. Since the C-terminal end of the protein is critical for the stabilization of the frataxin fold, the predictions presented may be reporting on the microscopic origin of the decrease in global stability produced near neutral pH in the psychrophilic variant. We propose that suboptimal electrostatic interactions may have been an evolutionary strategy for the adaptation of frataxin flexibility and function to cold environments.
Fil: Roman, Ernesto Andres. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Faraj, Santiago Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Cousido Siah, Alexandra. Université de Strasbourg; Francia
Fil: Mitschler, André. Université de Strasbourg; Francia
Fil: Podjarny, Alberto Daniel. Université de Strasbourg; Francia
Fil: Santos, Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
description Adaptation of life to low temperatures influences both protein stability and flexibility. Thus, proteins from psychrophilic organisms are excellent models to study relations between these properties. Here we focused on frataxin from Psychromonas ingrahamii (pFXN), an extreme psychrophilic sea ice bacterium that can grow at temperatures as low as - 12 C. This α/β protein is highly conserved and plays a key role in iron homeostasis as an iron chaperone. In contrast to other frataxin homologs, chemical and temperature unfolding experiments showed that the thermodynamic stability of pFXN is strongly modulated by pHs: Ranging from 5.5 ± 0.9 (pH 6.0) to 0.9 ± 0.3 kcal mol- 1 (pH 8.0). This protein was crystallized and its X-ray structure solved at 1.45 Å. Comparison of B-factor profiles between Escherichia coli and P. ingrahamii frataxin variants (51% of identity) suggests that, although both proteins share the same structural features, their flexibility distribution is different. Molecular dynamics simulations showed that protonation of His44 or His67 in pFXN lowers the mobility of regions encompassing residues 20-30 and the C-terminal end, probably through favorable electrostatic interactions with residues Asp27, Glu42 and Glu99. Since the C-terminal end of the protein is critical for the stabilization of the frataxin fold, the predictions presented may be reporting on the microscopic origin of the decrease in global stability produced near neutral pH in the psychrophilic variant. We propose that suboptimal electrostatic interactions may have been an evolutionary strategy for the adaptation of frataxin flexibility and function to cold environments.
publishDate 2013
dc.date.none.fl_str_mv 2013-06
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/11336/84739
Roman, Ernesto Andres; Faraj, Santiago Enrique; Cousido Siah, Alexandra; Mitschler, André; Podjarny, Alberto Daniel; et al.; Frataxin from Psychromonas ingrahamii as a model to study stability modulation within the CyaY protein family; Elsevier Science; Biochimica Et Biophysica Acta-proteins And Proteomics; 1834; 6; 6-2013; 1168-1180
1570-9639
CONICET Digital
CONICET
url http://hdl.handle.net/11336/84739
identifier_str_mv Roman, Ernesto Andres; Faraj, Santiago Enrique; Cousido Siah, Alexandra; Mitschler, André; Podjarny, Alberto Daniel; et al.; Frataxin from Psychromonas ingrahamii as a model to study stability modulation within the CyaY protein family; Elsevier Science; Biochimica Et Biophysica Acta-proteins And Proteomics; 1834; 6; 6-2013; 1168-1180
1570-9639
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://www.sciencedirect.com/science/article/pii/S1570963913000782
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbapap.2013.02.015
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
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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