Conformational Flexibility Drives Cold Adaptation in Pseudoalteromonas haloplanktis TAC125 Globins
Significance: Temperature is one of the most important drivers in shaping protein adaptations. Many biochemical and physiological processes are influenced by temperature. Proteins and enzymes from organisms living at low temperature are less stable in comparison to high-temperature adapted proteins....
Published in: | Antioxidants & Redox Signaling |
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Mary Ann Liebert
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ftconicet:oai:ri.conicet.gov.ar:11336/123695 2023-10-09T21:44:58+02:00 Conformational Flexibility Drives Cold Adaptation in Pseudoalteromonas haloplanktis TAC125 Globins Giordano, Daniela Boubeta, Fernando Martín di Prisco, Guido Estrin, Dario Ariel Smulevich, Giulietta Viappiani, Christiano Verde, Cinzia application/pdf http://hdl.handle.net/11336/123695 eng eng Mary Ann Liebert info:eu-repo/semantics/altIdentifier/url/https://www.liebertpub.com/doi/10.1089/ars.2019.7887 info:eu-repo/semantics/altIdentifier/doi/10.1089/ars.2019.7887 http://hdl.handle.net/11336/123695 Giordano, Daniela; Boubeta, Fernando Martín; di Prisco, Guido; Estrin, Dario Ariel; Smulevich, Giulietta; et al.; Conformational Flexibility Drives Cold Adaptation in Pseudoalteromonas haloplanktis TAC125 Globins; Mary Ann Liebert; Antioxidants & Redox Signaling; 32; 6; 10-2019; 396-411 1523-0864 CONICET Digital CONICET info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ BACTERIAL GLOBIN HEME-POCKET FLEXIBILITY HEXA-COORDINATION OXIDATIVE/NITROSATIVE STRESS THERMAL ADAPTATION 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/10.1089/ars.2019.7887 2023-09-24T20:17:08Z Significance: Temperature is one of the most important drivers in shaping protein adaptations. Many biochemical and physiological processes are influenced by temperature. Proteins and enzymes from organisms living at low temperature are less stable in comparison to high-temperature adapted proteins. The lower stability is generally due to greater conformational flexibility. Recent Advances: Adaptive changes in the structure of cold-adapted proteins may occur at subunit interfaces, distant from the active site, thus producing energy changes associated with conformational transitions transmitted to the active site by allosteric modulation, valid also for monomeric proteins in which tertiary structural changes may play an essential role. Critical Issues: Despite efforts, the current experimental and computational methods still fail to produce general principles on protein evolution, since many changes are protein and species dependent. Environmental constraints or other biological cellular signals may override the ancestral information included in the structure of the protein, thus introducing inaccuracy in estimates and predictions on the evolutionary adaptations of proteins in response to cold adaptation. Future Directions: In this review, we describe the studies and approaches used to investigate stability and flexibility in the cold-adapted globins of the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125. In fact, future research directions will be prescient on more detailed investigation of cold-adapted proteins and the role of fluctuations between different conformational states. Fil: Giordano, Daniela. Institute Of Biosciences And Bioresources; Italia Fil: Boubeta, Fernando Martín. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, ... Article in Journal/Newspaper Antarc* Antarctic CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) Antarctic The Antarctic Antioxidants & Redox Signaling 32 6 396 411 |
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CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) |
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language |
English |
topic |
BACTERIAL GLOBIN HEME-POCKET FLEXIBILITY HEXA-COORDINATION OXIDATIVE/NITROSATIVE STRESS THERMAL ADAPTATION https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
spellingShingle |
BACTERIAL GLOBIN HEME-POCKET FLEXIBILITY HEXA-COORDINATION OXIDATIVE/NITROSATIVE STRESS THERMAL ADAPTATION https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 Giordano, Daniela Boubeta, Fernando Martín di Prisco, Guido Estrin, Dario Ariel Smulevich, Giulietta Viappiani, Christiano Verde, Cinzia Conformational Flexibility Drives Cold Adaptation in Pseudoalteromonas haloplanktis TAC125 Globins |
topic_facet |
BACTERIAL GLOBIN HEME-POCKET FLEXIBILITY HEXA-COORDINATION OXIDATIVE/NITROSATIVE STRESS THERMAL ADAPTATION https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
description |
Significance: Temperature is one of the most important drivers in shaping protein adaptations. Many biochemical and physiological processes are influenced by temperature. Proteins and enzymes from organisms living at low temperature are less stable in comparison to high-temperature adapted proteins. The lower stability is generally due to greater conformational flexibility. Recent Advances: Adaptive changes in the structure of cold-adapted proteins may occur at subunit interfaces, distant from the active site, thus producing energy changes associated with conformational transitions transmitted to the active site by allosteric modulation, valid also for monomeric proteins in which tertiary structural changes may play an essential role. Critical Issues: Despite efforts, the current experimental and computational methods still fail to produce general principles on protein evolution, since many changes are protein and species dependent. Environmental constraints or other biological cellular signals may override the ancestral information included in the structure of the protein, thus introducing inaccuracy in estimates and predictions on the evolutionary adaptations of proteins in response to cold adaptation. Future Directions: In this review, we describe the studies and approaches used to investigate stability and flexibility in the cold-adapted globins of the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125. In fact, future research directions will be prescient on more detailed investigation of cold-adapted proteins and the role of fluctuations between different conformational states. Fil: Giordano, Daniela. Institute Of Biosciences And Bioresources; Italia Fil: Boubeta, Fernando Martín. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, ... |
format |
Article in Journal/Newspaper |
author |
Giordano, Daniela Boubeta, Fernando Martín di Prisco, Guido Estrin, Dario Ariel Smulevich, Giulietta Viappiani, Christiano Verde, Cinzia |
author_facet |
Giordano, Daniela Boubeta, Fernando Martín di Prisco, Guido Estrin, Dario Ariel Smulevich, Giulietta Viappiani, Christiano Verde, Cinzia |
author_sort |
Giordano, Daniela |
title |
Conformational Flexibility Drives Cold Adaptation in Pseudoalteromonas haloplanktis TAC125 Globins |
title_short |
Conformational Flexibility Drives Cold Adaptation in Pseudoalteromonas haloplanktis TAC125 Globins |
title_full |
Conformational Flexibility Drives Cold Adaptation in Pseudoalteromonas haloplanktis TAC125 Globins |
title_fullStr |
Conformational Flexibility Drives Cold Adaptation in Pseudoalteromonas haloplanktis TAC125 Globins |
title_full_unstemmed |
Conformational Flexibility Drives Cold Adaptation in Pseudoalteromonas haloplanktis TAC125 Globins |
title_sort |
conformational flexibility drives cold adaptation in pseudoalteromonas haloplanktis tac125 globins |
publisher |
Mary Ann Liebert |
url |
http://hdl.handle.net/11336/123695 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
info:eu-repo/semantics/altIdentifier/url/https://www.liebertpub.com/doi/10.1089/ars.2019.7887 info:eu-repo/semantics/altIdentifier/doi/10.1089/ars.2019.7887 http://hdl.handle.net/11336/123695 Giordano, Daniela; Boubeta, Fernando Martín; di Prisco, Guido; Estrin, Dario Ariel; Smulevich, Giulietta; et al.; Conformational Flexibility Drives Cold Adaptation in Pseudoalteromonas haloplanktis TAC125 Globins; Mary Ann Liebert; Antioxidants & Redox Signaling; 32; 6; 10-2019; 396-411 1523-0864 CONICET Digital CONICET |
op_rights |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
op_doi |
https://doi.org/10.1089/ars.2019.7887 |
container_title |
Antioxidants & Redox Signaling |
container_volume |
32 |
container_issue |
6 |
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396 |
op_container_end_page |
411 |
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1779314997239742464 |