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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/84739
Ver los metadatos del registro completo
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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 Técnicas2025-09-29T10:20:12Zoai: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:34982025-09-29 10:20:12.486CONICET 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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13.070432 |