Copper resistance in the cold: Genome analysis and characterisation of a P IB‐1 ATPase in Bizionia argentinensis

Autores
Burgardt, Noelia Ines; Melian, Noelia Agostina; Gonzalez Flecha, Francisco Luis
Año de publicación
2024
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Copper homeostasis is a key process in organisms, with distinctive pathways that have developed according to specific needs but conserve the main resistance mechanisms. These systems are well described in model bacterium, but there is little information about copper resistance in species adapted to cold environments. In this work we explore the repertoire of genes that might be related to copper homeostasis in the genome of Bizionia argentinensis (JUB59-T), a psychrotolerant bacteria isolated from the Antarctic sea water. Several genes were found encoding proteins similar to well-known proteins essential for copper homeostasis, including three sequences of copper-transport P1B-type ATPases. We selected one of these, denoted as BaCopA1, for cloning and expression in Saccharomyces cerevisiae. BaCopA1 was successfully incorporated into yeasts membranes, from where it was removed with detergent. Purified BaCopA1 catalyzes ATP hydrolysis at low temperature. The structural models of different BaCopA1 conformations were obtained and compared to the mesophilic and thermophilic homologous structures. The high conservation of essential residues and the structural similarity between these proteins suggest that they share the same reaction mechanism for copper transport. This is the first report of a psychrotolerant P1B-ATPase expressed and purified in a functional form.
Fil: Burgardt, Noelia Ines. 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: Melian, Noelia Agostina. 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: Gonzalez Flecha, Francisco Luis. 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
COPPER REGULATION
ANTARTIC BACTERIA
PSYCHROTOLERANT ENZYMES
COPPER P-ATPASES
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/239980

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network_name_str CONICET Digital (CONICET)
spelling Copper resistance in the cold: Genome analysis and characterisation of a P IB‐1 ATPase in Bizionia argentinensisBurgardt, Noelia InesMelian, Noelia AgostinaGonzalez Flecha, Francisco LuisCOPPER REGULATIONANTARTIC BACTERIAPSYCHROTOLERANT ENZYMESCOPPER P-ATPASEShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Copper homeostasis is a key process in organisms, with distinctive pathways that have developed according to specific needs but conserve the main resistance mechanisms. These systems are well described in model bacterium, but there is little information about copper resistance in species adapted to cold environments. In this work we explore the repertoire of genes that might be related to copper homeostasis in the genome of Bizionia argentinensis (JUB59-T), a psychrotolerant bacteria isolated from the Antarctic sea water. Several genes were found encoding proteins similar to well-known proteins essential for copper homeostasis, including three sequences of copper-transport P1B-type ATPases. We selected one of these, denoted as BaCopA1, for cloning and expression in Saccharomyces cerevisiae. BaCopA1 was successfully incorporated into yeasts membranes, from where it was removed with detergent. Purified BaCopA1 catalyzes ATP hydrolysis at low temperature. The structural models of different BaCopA1 conformations were obtained and compared to the mesophilic and thermophilic homologous structures. The high conservation of essential residues and the structural similarity between these proteins suggest that they share the same reaction mechanism for copper transport. This is the first report of a psychrotolerant P1B-ATPase expressed and purified in a functional form.Fil: Burgardt, Noelia Ines. 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: Melian, Noelia Agostina. 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: Gonzalez Flecha, Francisco Luis. 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; ArgentinaWiley2024-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/239980Burgardt, Noelia Ines; Melian, Noelia Agostina; Gonzalez Flecha, Francisco Luis; Copper resistance in the cold: Genome analysis and characterisation of a P IB‐1 ATPase in Bizionia argentinensis; Wiley; Environmental Microbiology Reports; 16; 4; 6-2024; 1-161758-2229CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://enviromicro-journals.onlinelibrary.wiley.com/doi/10.1111/1758-2229.13278info:eu-repo/semantics/altIdentifier/doi/10.1111/1758-2229.13278info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:06:34Zoai:ri.conicet.gov.ar:11336/239980instacron: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 10:06:34.299CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Copper resistance in the cold: Genome analysis and characterisation of a P IB‐1 ATPase in Bizionia argentinensis
title Copper resistance in the cold: Genome analysis and characterisation of a P IB‐1 ATPase in Bizionia argentinensis
spellingShingle Copper resistance in the cold: Genome analysis and characterisation of a P IB‐1 ATPase in Bizionia argentinensis
Burgardt, Noelia Ines
COPPER REGULATION
ANTARTIC BACTERIA
PSYCHROTOLERANT ENZYMES
COPPER P-ATPASES
title_short Copper resistance in the cold: Genome analysis and characterisation of a P IB‐1 ATPase in Bizionia argentinensis
title_full Copper resistance in the cold: Genome analysis and characterisation of a P IB‐1 ATPase in Bizionia argentinensis
title_fullStr Copper resistance in the cold: Genome analysis and characterisation of a P IB‐1 ATPase in Bizionia argentinensis
title_full_unstemmed Copper resistance in the cold: Genome analysis and characterisation of a P IB‐1 ATPase in Bizionia argentinensis
title_sort Copper resistance in the cold: Genome analysis and characterisation of a P IB‐1 ATPase in Bizionia argentinensis
dc.creator.none.fl_str_mv Burgardt, Noelia Ines
Melian, Noelia Agostina
Gonzalez Flecha, Francisco Luis
author Burgardt, Noelia Ines
author_facet Burgardt, Noelia Ines
Melian, Noelia Agostina
Gonzalez Flecha, Francisco Luis
author_role author
author2 Melian, Noelia Agostina
Gonzalez Flecha, Francisco Luis
author2_role author
author
dc.subject.none.fl_str_mv COPPER REGULATION
ANTARTIC BACTERIA
PSYCHROTOLERANT ENZYMES
COPPER P-ATPASES
topic COPPER REGULATION
ANTARTIC BACTERIA
PSYCHROTOLERANT ENZYMES
COPPER P-ATPASES
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Copper homeostasis is a key process in organisms, with distinctive pathways that have developed according to specific needs but conserve the main resistance mechanisms. These systems are well described in model bacterium, but there is little information about copper resistance in species adapted to cold environments. In this work we explore the repertoire of genes that might be related to copper homeostasis in the genome of Bizionia argentinensis (JUB59-T), a psychrotolerant bacteria isolated from the Antarctic sea water. Several genes were found encoding proteins similar to well-known proteins essential for copper homeostasis, including three sequences of copper-transport P1B-type ATPases. We selected one of these, denoted as BaCopA1, for cloning and expression in Saccharomyces cerevisiae. BaCopA1 was successfully incorporated into yeasts membranes, from where it was removed with detergent. Purified BaCopA1 catalyzes ATP hydrolysis at low temperature. The structural models of different BaCopA1 conformations were obtained and compared to the mesophilic and thermophilic homologous structures. The high conservation of essential residues and the structural similarity between these proteins suggest that they share the same reaction mechanism for copper transport. This is the first report of a psychrotolerant P1B-ATPase expressed and purified in a functional form.
Fil: Burgardt, Noelia Ines. 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: Melian, Noelia Agostina. 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: Gonzalez Flecha, Francisco Luis. 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 Copper homeostasis is a key process in organisms, with distinctive pathways that have developed according to specific needs but conserve the main resistance mechanisms. These systems are well described in model bacterium, but there is little information about copper resistance in species adapted to cold environments. In this work we explore the repertoire of genes that might be related to copper homeostasis in the genome of Bizionia argentinensis (JUB59-T), a psychrotolerant bacteria isolated from the Antarctic sea water. Several genes were found encoding proteins similar to well-known proteins essential for copper homeostasis, including three sequences of copper-transport P1B-type ATPases. We selected one of these, denoted as BaCopA1, for cloning and expression in Saccharomyces cerevisiae. BaCopA1 was successfully incorporated into yeasts membranes, from where it was removed with detergent. Purified BaCopA1 catalyzes ATP hydrolysis at low temperature. The structural models of different BaCopA1 conformations were obtained and compared to the mesophilic and thermophilic homologous structures. The high conservation of essential residues and the structural similarity between these proteins suggest that they share the same reaction mechanism for copper transport. This is the first report of a psychrotolerant P1B-ATPase expressed and purified in a functional form.
publishDate 2024
dc.date.none.fl_str_mv 2024-06
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/11336/239980
Burgardt, Noelia Ines; Melian, Noelia Agostina; Gonzalez Flecha, Francisco Luis; Copper resistance in the cold: Genome analysis and characterisation of a P IB‐1 ATPase in Bizionia argentinensis; Wiley; Environmental Microbiology Reports; 16; 4; 6-2024; 1-16
1758-2229
CONICET Digital
CONICET
url http://hdl.handle.net/11336/239980
identifier_str_mv Burgardt, Noelia Ines; Melian, Noelia Agostina; Gonzalez Flecha, Francisco Luis; Copper resistance in the cold: Genome analysis and characterisation of a P IB‐1 ATPase in Bizionia argentinensis; Wiley; Environmental Microbiology Reports; 16; 4; 6-2024; 1-16
1758-2229
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://enviromicro-journals.onlinelibrary.wiley.com/doi/10.1111/1758-2229.13278
info:eu-repo/semantics/altIdentifier/doi/10.1111/1758-2229.13278
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley
publisher.none.fl_str_mv Wiley
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
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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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