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...
Published in: | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics |
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Online Access: | https://hal.science/hal-04611732 https://doi.org/10.1016/j.bbapap.2013.02.015 |
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ftinserm:oai:HAL:hal-04611732v1 2024-09-15T18:35:33+00:00 Frataxin from Psychromonas ingrahamii as a model to study stability modulation within the CyaY protein family Roman, Ernesto A. Faraj, Santiago E. Cousido-Siah, Alexandra Mitschler, André Podjarny, Alberto Santos, Javier Universidad de Buenos Aires Buenos Aires (UBA) Institut de génétique et biologie moléculaire et cellulaire (IGBMC) Université Louis Pasteur - Strasbourg I-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS) 2013 https://hal.science/hal-04611732 https://doi.org/10.1016/j.bbapap.2013.02.015 en eng HAL CCSD Elsevier info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbapap.2013.02.015 info:eu-repo/semantics/altIdentifier/pmid/23429177 hal-04611732 https://hal.science/hal-04611732 doi:10.1016/j.bbapap.2013.02.015 PUBMED: 23429177 ISSN: 0006-3002 BBA - Biochimica et Biophysica Acta https://hal.science/hal-04611732 BBA - Biochimica et Biophysica Acta, 2013, 1834 (6), pp.1168-1180. ⟨10.1016/j.bbapap.2013.02.015⟩ http://www.ncbi.nlm.nih.gov/pubmed/23429177 [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology info:eu-repo/semantics/article Journal articles 2013 ftinserm https://doi.org/10.1016/j.bbapap.2013.02.015 2024-07-01T23:41:43Z 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 degrees C. This alpha/beta 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 (pH6.0) to 0.9+/-0.3kcalmol(-1) (pH8.0). This protein was crystallized and its X-ray structure solved at 1.45A. 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. Article in Journal/Newspaper Sea ice Inserm: HAL (Institut national de la santé et de la recherche médicale) Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1834 6 1168 1180 |
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Open Polar |
collection |
Inserm: HAL (Institut national de la santé et de la recherche médicale) |
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ftinserm |
language |
English |
topic |
[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology |
spellingShingle |
[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Roman, Ernesto A. Faraj, Santiago E. Cousido-Siah, Alexandra Mitschler, André Podjarny, Alberto Santos, Javier Frataxin from Psychromonas ingrahamii as a model to study stability modulation within the CyaY protein family |
topic_facet |
[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology |
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 degrees C. This alpha/beta 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 (pH6.0) to 0.9+/-0.3kcalmol(-1) (pH8.0). This protein was crystallized and its X-ray structure solved at 1.45A. 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. |
author2 |
Universidad de Buenos Aires Buenos Aires (UBA) Institut de génétique et biologie moléculaire et cellulaire (IGBMC) Université Louis Pasteur - Strasbourg I-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS) |
format |
Article in Journal/Newspaper |
author |
Roman, Ernesto A. Faraj, Santiago E. Cousido-Siah, Alexandra Mitschler, André Podjarny, Alberto Santos, Javier |
author_facet |
Roman, Ernesto A. Faraj, Santiago E. Cousido-Siah, Alexandra Mitschler, André Podjarny, Alberto Santos, Javier |
author_sort |
Roman, Ernesto A. |
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 |
HAL CCSD |
publishDate |
2013 |
url |
https://hal.science/hal-04611732 https://doi.org/10.1016/j.bbapap.2013.02.015 |
genre |
Sea ice |
genre_facet |
Sea ice |
op_source |
ISSN: 0006-3002 BBA - Biochimica et Biophysica Acta https://hal.science/hal-04611732 BBA - Biochimica et Biophysica Acta, 2013, 1834 (6), pp.1168-1180. ⟨10.1016/j.bbapap.2013.02.015⟩ http://www.ncbi.nlm.nih.gov/pubmed/23429177 |
op_relation |
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbapap.2013.02.015 info:eu-repo/semantics/altIdentifier/pmid/23429177 hal-04611732 https://hal.science/hal-04611732 doi:10.1016/j.bbapap.2013.02.015 PUBMED: 23429177 |
op_doi |
https://doi.org/10.1016/j.bbapap.2013.02.015 |
container_title |
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics |
container_volume |
1834 |
container_issue |
6 |
container_start_page |
1168 |
op_container_end_page |
1180 |
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1810478736641884160 |