Frataxin from Psychromonas ingrahamii as a model to study stability modulation within the CyaY protein family
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 ba...
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ftconicet:oai:ri.conicet.gov.ar:11336/84739 2023-10-09T21:55:53+02:00 Frataxin from Psychromonas ingrahamii as a model to study stability modulation within the CyaY protein family Roman, Ernesto Andres Faraj, Santiago Enrique Cousido Siah, Alexandra Mitschler, André Podjarny, Alberto Daniel Santos, Javier application/pdf http://hdl.handle.net/11336/84739 eng eng Elsevier Science 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 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 info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ CRYSTALLOGRAPHY MOLECULAR DYNAMICS SIMULATIONS PROTEIN DYNAMICS PROTEIN FLEXIBILITY PROTEIN STABILITY STABILITY MODULATION https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion ftconicet https://doi.org/10.1016/j.bbapap.2013.02.015 2023-09-24T19:50:46Z 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. ... Article in Journal/Newspaper Sea ice CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) Argentina Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1834 6 1168 1180 |
institution |
Open Polar |
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CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) |
op_collection_id |
ftconicet |
language |
English |
topic |
CRYSTALLOGRAPHY MOLECULAR DYNAMICS SIMULATIONS PROTEIN DYNAMICS PROTEIN FLEXIBILITY PROTEIN STABILITY STABILITY MODULATION https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
spellingShingle |
CRYSTALLOGRAPHY MOLECULAR DYNAMICS SIMULATIONS PROTEIN DYNAMICS PROTEIN FLEXIBILITY PROTEIN STABILITY STABILITY MODULATION https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 Roman, Ernesto Andres Faraj, Santiago Enrique Cousido Siah, Alexandra Mitschler, André Podjarny, Alberto Daniel Santos, Javier Frataxin from Psychromonas ingrahamii as a model to study stability modulation within the CyaY protein family |
topic_facet |
CRYSTALLOGRAPHY MOLECULAR DYNAMICS SIMULATIONS PROTEIN DYNAMICS PROTEIN FLEXIBILITY PROTEIN STABILITY STABILITY MODULATION https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
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. 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. ... |
format |
Article in Journal/Newspaper |
author |
Roman, Ernesto Andres Faraj, Santiago Enrique Cousido Siah, Alexandra Mitschler, André Podjarny, Alberto Daniel Santos, Javier |
author_facet |
Roman, Ernesto Andres Faraj, Santiago Enrique Cousido Siah, Alexandra Mitschler, André Podjarny, Alberto Daniel Santos, Javier |
author_sort |
Roman, Ernesto Andres |
title |
Frataxin from Psychromonas ingrahamii as a model to study stability modulation within the CyaY protein family |
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 |
publisher |
Elsevier Science |
url |
http://hdl.handle.net/11336/84739 |
geographic |
Argentina |
geographic_facet |
Argentina |
genre |
Sea ice |
genre_facet |
Sea ice |
op_relation |
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 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 |
op_rights |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
op_doi |
https://doi.org/10.1016/j.bbapap.2013.02.015 |
container_title |
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics |
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1834 |
container_issue |
6 |
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1168 |
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1180 |
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1779320115194494976 |