Looking for the mechanism of arsenate respiration of Fusibacter sp. strain 3D3, independent of ArrAB

Autores
Acosta Grinok, Mauricio; Vázquez, Susana Claudia; Guiliani, Nicolás; Marín, Sabrina; Demergasso, Cecilia
Año de publicación
2022
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The literature has reported the isolation of arsenate-dependent growing microorganisms which lack a canonical homolog for respiratory arsenate reductase, ArrAB. We recently isolated an arsenate-dependent growing bacterium from volcanic arsenic-bearing environments in Northern Chile, Fusibacter sp. strain 3D3 (Fas) and studied the arsenic metabolism in this Gram-positive isolate. Features of Fas deduced from genome analysis and comparative analysis with other arsenate-reducing microorganisms revealed the lack of ArrAB coding genes and the occurrence of two arsC genes encoding for putative cytoplasmic arsenate reductases named ArsC-1 and ArsC-2. Interestingly, ArsC-1 and ArsC-2 belong to the thioredoxin-coupled family (because of the redox-active disulfide protein used as reductant), but they conferred differential arsenate resistance to the E. coli WC3110 ΔarsC strain. PCR experiments confirmed the absence of arrAB genes and results obtained using uncouplers revealed that Fas growth is linked to the proton gradient. In addition, Fas harbors ferredoxin-NAD+ oxidoreductase (Rnf) and electron transfer flavoprotein (etf) coding genes. These are key molecular markers of a recently discovered flavin-based electron bifurcation mechanism involved in energy conservation, mainly in anaerobic metabolisms regulated by the cellular redox state and mostly associated with cytoplasmic enzyme complexes. At least three electron-bifurcating flavoenzyme complexes were evidenced in Fas, some of them shared in conserved genomic regions by other members of the Fusibacter genus. These physiological and genomic findings permit us to hypothesize the existence of an uncharacterized arsenate-dependent growth metabolism regulated by the cellular redox state in the Fusibacter genus.
Fil: Acosta Grinok, Mauricio. Universidad Católica del Norte; Chile
Fil: Vázquez, Susana Claudia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Microbiología, Inmunología y Biotecnología. Cátedra de Microbiología Industrial y Biotecnología; Argentina
Fil: Guiliani, Nicolás. Universidad de Chile; Chile
Fil: Marín, Sabrina. Universidad Católica del Norte; Chile
Fil: Demergasso, Cecilia. Universidad Católica del Norte; Chile
Materia
ARSENIC RESPIRATION
ELECTRON BIFURCATION
ETF
FERREDOXIN
FUSIBACTER
NORTHERN CHILE
RNF COMPLEX
THIOREDOXIN
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/214419
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Looking for the mechanism of arsenate respiration of Fusibacter sp. strain 3D3, independent of ArrABAcosta Grinok, MauricioVázquez, Susana ClaudiaGuiliani, NicolásMarín, SabrinaDemergasso, CeciliaARSENIC RESPIRATIONELECTRON BIFURCATIONETFFERREDOXINFUSIBACTERNORTHERN CHILERNF COMPLEXTHIOREDOXINhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The literature has reported the isolation of arsenate-dependent growing microorganisms which lack a canonical homolog for respiratory arsenate reductase, ArrAB. We recently isolated an arsenate-dependent growing bacterium from volcanic arsenic-bearing environments in Northern Chile, Fusibacter sp. strain 3D3 (Fas) and studied the arsenic metabolism in this Gram-positive isolate. Features of Fas deduced from genome analysis and comparative analysis with other arsenate-reducing microorganisms revealed the lack of ArrAB coding genes and the occurrence of two arsC genes encoding for putative cytoplasmic arsenate reductases named ArsC-1 and ArsC-2. Interestingly, ArsC-1 and ArsC-2 belong to the thioredoxin-coupled family (because of the redox-active disulfide protein used as reductant), but they conferred differential arsenate resistance to the E. coli WC3110 ΔarsC strain. PCR experiments confirmed the absence of arrAB genes and results obtained using uncouplers revealed that Fas growth is linked to the proton gradient. In addition, Fas harbors ferredoxin-NAD+ oxidoreductase (Rnf) and electron transfer flavoprotein (etf) coding genes. These are key molecular markers of a recently discovered flavin-based electron bifurcation mechanism involved in energy conservation, mainly in anaerobic metabolisms regulated by the cellular redox state and mostly associated with cytoplasmic enzyme complexes. At least three electron-bifurcating flavoenzyme complexes were evidenced in Fas, some of them shared in conserved genomic regions by other members of the Fusibacter genus. These physiological and genomic findings permit us to hypothesize the existence of an uncharacterized arsenate-dependent growth metabolism regulated by the cellular redox state in the Fusibacter genus.Fil: Acosta Grinok, Mauricio. Universidad Católica del Norte; ChileFil: Vázquez, Susana Claudia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Microbiología, Inmunología y Biotecnología. Cátedra de Microbiología Industrial y Biotecnología; ArgentinaFil: Guiliani, Nicolás. Universidad de Chile; ChileFil: Marín, Sabrina. Universidad Católica del Norte; ChileFil: Demergasso, Cecilia. Universidad Católica del Norte; ChileFrontiers Media2022-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/214419Acosta Grinok, Mauricio; Vázquez, Susana Claudia; Guiliani, Nicolás; Marín, Sabrina; Demergasso, Cecilia; Looking for the mechanism of arsenate respiration of Fusibacter sp. strain 3D3, independent of ArrAB; Frontiers Media; Frontiers in Microbiology; 13; 12-2022; 1-281664-302XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.frontiersin.org/articles/10.3389/fmicb.2022.1029886/fullinfo:eu-repo/semantics/altIdentifier/doi/10.3389/fmicb.2022.1029886info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-11-12T10:00:11Zoai:ri.conicet.gov.ar:11336/214419instacron: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:34982025-11-12 10:00:11.639CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Looking for the mechanism of arsenate respiration of Fusibacter sp. strain 3D3, independent of ArrAB
title Looking for the mechanism of arsenate respiration of Fusibacter sp. strain 3D3, independent of ArrAB
spellingShingle Looking for the mechanism of arsenate respiration of Fusibacter sp. strain 3D3, independent of ArrAB
Acosta Grinok, Mauricio
ARSENIC RESPIRATION
ELECTRON BIFURCATION
ETF
FERREDOXIN
FUSIBACTER
NORTHERN CHILE
RNF COMPLEX
THIOREDOXIN
title_short Looking for the mechanism of arsenate respiration of Fusibacter sp. strain 3D3, independent of ArrAB
title_full Looking for the mechanism of arsenate respiration of Fusibacter sp. strain 3D3, independent of ArrAB
title_fullStr Looking for the mechanism of arsenate respiration of Fusibacter sp. strain 3D3, independent of ArrAB
title_full_unstemmed Looking for the mechanism of arsenate respiration of Fusibacter sp. strain 3D3, independent of ArrAB
title_sort Looking for the mechanism of arsenate respiration of Fusibacter sp. strain 3D3, independent of ArrAB
dc.creator.none.fl_str_mv Acosta Grinok, Mauricio
Vázquez, Susana Claudia
Guiliani, Nicolás
Marín, Sabrina
Demergasso, Cecilia
author Acosta Grinok, Mauricio
author_facet Acosta Grinok, Mauricio
Vázquez, Susana Claudia
Guiliani, Nicolás
Marín, Sabrina
Demergasso, Cecilia
author_role author
author2 Vázquez, Susana Claudia
Guiliani, Nicolás
Marín, Sabrina
Demergasso, Cecilia
author2_role author
author
author
author
dc.subject.none.fl_str_mv ARSENIC RESPIRATION
ELECTRON BIFURCATION
ETF
FERREDOXIN
FUSIBACTER
NORTHERN CHILE
RNF COMPLEX
THIOREDOXIN
topic ARSENIC RESPIRATION
ELECTRON BIFURCATION
ETF
FERREDOXIN
FUSIBACTER
NORTHERN CHILE
RNF COMPLEX
THIOREDOXIN
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The literature has reported the isolation of arsenate-dependent growing microorganisms which lack a canonical homolog for respiratory arsenate reductase, ArrAB. We recently isolated an arsenate-dependent growing bacterium from volcanic arsenic-bearing environments in Northern Chile, Fusibacter sp. strain 3D3 (Fas) and studied the arsenic metabolism in this Gram-positive isolate. Features of Fas deduced from genome analysis and comparative analysis with other arsenate-reducing microorganisms revealed the lack of ArrAB coding genes and the occurrence of two arsC genes encoding for putative cytoplasmic arsenate reductases named ArsC-1 and ArsC-2. Interestingly, ArsC-1 and ArsC-2 belong to the thioredoxin-coupled family (because of the redox-active disulfide protein used as reductant), but they conferred differential arsenate resistance to the E. coli WC3110 ΔarsC strain. PCR experiments confirmed the absence of arrAB genes and results obtained using uncouplers revealed that Fas growth is linked to the proton gradient. In addition, Fas harbors ferredoxin-NAD+ oxidoreductase (Rnf) and electron transfer flavoprotein (etf) coding genes. These are key molecular markers of a recently discovered flavin-based electron bifurcation mechanism involved in energy conservation, mainly in anaerobic metabolisms regulated by the cellular redox state and mostly associated with cytoplasmic enzyme complexes. At least three electron-bifurcating flavoenzyme complexes were evidenced in Fas, some of them shared in conserved genomic regions by other members of the Fusibacter genus. These physiological and genomic findings permit us to hypothesize the existence of an uncharacterized arsenate-dependent growth metabolism regulated by the cellular redox state in the Fusibacter genus.
Fil: Acosta Grinok, Mauricio. Universidad Católica del Norte; Chile
Fil: Vázquez, Susana Claudia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Microbiología, Inmunología y Biotecnología. Cátedra de Microbiología Industrial y Biotecnología; Argentina
Fil: Guiliani, Nicolás. Universidad de Chile; Chile
Fil: Marín, Sabrina. Universidad Católica del Norte; Chile
Fil: Demergasso, Cecilia. Universidad Católica del Norte; Chile
description The literature has reported the isolation of arsenate-dependent growing microorganisms which lack a canonical homolog for respiratory arsenate reductase, ArrAB. We recently isolated an arsenate-dependent growing bacterium from volcanic arsenic-bearing environments in Northern Chile, Fusibacter sp. strain 3D3 (Fas) and studied the arsenic metabolism in this Gram-positive isolate. Features of Fas deduced from genome analysis and comparative analysis with other arsenate-reducing microorganisms revealed the lack of ArrAB coding genes and the occurrence of two arsC genes encoding for putative cytoplasmic arsenate reductases named ArsC-1 and ArsC-2. Interestingly, ArsC-1 and ArsC-2 belong to the thioredoxin-coupled family (because of the redox-active disulfide protein used as reductant), but they conferred differential arsenate resistance to the E. coli WC3110 ΔarsC strain. PCR experiments confirmed the absence of arrAB genes and results obtained using uncouplers revealed that Fas growth is linked to the proton gradient. In addition, Fas harbors ferredoxin-NAD+ oxidoreductase (Rnf) and electron transfer flavoprotein (etf) coding genes. These are key molecular markers of a recently discovered flavin-based electron bifurcation mechanism involved in energy conservation, mainly in anaerobic metabolisms regulated by the cellular redox state and mostly associated with cytoplasmic enzyme complexes. At least three electron-bifurcating flavoenzyme complexes were evidenced in Fas, some of them shared in conserved genomic regions by other members of the Fusibacter genus. These physiological and genomic findings permit us to hypothesize the existence of an uncharacterized arsenate-dependent growth metabolism regulated by the cellular redox state in the Fusibacter genus.
publishDate 2022
dc.date.none.fl_str_mv 2022-12
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/11336/214419
Acosta Grinok, Mauricio; Vázquez, Susana Claudia; Guiliani, Nicolás; Marín, Sabrina; Demergasso, Cecilia; Looking for the mechanism of arsenate respiration of Fusibacter sp. strain 3D3, independent of ArrAB; Frontiers Media; Frontiers in Microbiology; 13; 12-2022; 1-28
1664-302X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/214419
identifier_str_mv Acosta Grinok, Mauricio; Vázquez, Susana Claudia; Guiliani, Nicolás; Marín, Sabrina; Demergasso, Cecilia; Looking for the mechanism of arsenate respiration of Fusibacter sp. strain 3D3, independent of ArrAB; Frontiers Media; Frontiers in Microbiology; 13; 12-2022; 1-28
1664-302X
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://www.frontiersin.org/articles/10.3389/fmicb.2022.1029886/full
info:eu-repo/semantics/altIdentifier/doi/10.3389/fmicb.2022.1029886
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Frontiers Media
publisher.none.fl_str_mv Frontiers Media
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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