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dc.contributor.author
Acosta Grinok, Mauricio
dc.contributor.author
Vázquez, Susana Claudia
dc.contributor.author
Guiliani, Nicolás
dc.contributor.author
Marín, Sabrina
dc.contributor.author
Demergasso, Cecilia
dc.date.available
2023-10-06T17:37:15Z
dc.date.issued
2022-12
dc.identifier.citation
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
dc.identifier.issn
1664-302X
dc.identifier.uri
http://hdl.handle.net/11336/214419
dc.description.abstract
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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Frontiers Media
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
ARSENIC RESPIRATION
dc.subject
ELECTRON BIFURCATION
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ETF
dc.subject
FERREDOXIN
dc.subject
FUSIBACTER
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NORTHERN CHILE
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RNF COMPLEX
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THIOREDOXIN
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Biología Celular, Microbiología
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Looking for the mechanism of arsenate respiration of Fusibacter sp. strain 3D3, independent of ArrAB
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2023-06-30T15:25:28Z
dc.journal.volume
13
dc.journal.pagination
1-28
dc.journal.pais
Suiza
dc.description.fil
Fil: Acosta Grinok, Mauricio. Universidad Católica del Norte; Chile
dc.description.fil
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
dc.description.fil
Fil: Guiliani, Nicolás. Universidad de Chile; Chile
dc.description.fil
Fil: Marín, Sabrina. Universidad Católica del Norte; Chile
dc.description.fil
Fil: Demergasso, Cecilia. Universidad Católica del Norte; Chile
dc.journal.title
Frontiers in Microbiology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.frontiersin.org/articles/10.3389/fmicb.2022.1029886/full
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.3389/fmicb.2022.1029886
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