bioRxivMicrobiologyPreprint
Looking for the mechanism of arsenate respiration in an arsenate-dependent growing culture of Fusibacter sp. strain 3D3, independent of ArrAB.
M. Acosta Grinox, S. Vazquez, N. S. Guiliani, S. A. Marin, C. S. Demergasso
Abstract
The literature has reported the isolation of arsenate-dependent growing (ADG) microorganisms which lack a canonical homolog for respiratory arsenate reductase, ArrAB. We recently isolated an ADG bacterium from 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 arsenic-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 AsV resistance to the E. coli WC3110 {Delta}arsC 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) 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 Fusibacter genus.
- organism: bacteria (other)
- research focus: host-pathogen & immune response
- approach: experimental assay
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Structure, interaction and post-translational modification study of arsenic reduction system in Bifidobacterium longum
Zarrin Basharat, Azra Yasmin·bioRxiv·Jul 27, 2016
- Defining the role of aerobic respiration in the metabolism and bioenergetics of Enterococcus faecalis
Olivia Paxie, Brunda Nijagal, … Rachel L. Darnell·bioRxiv·Aug 31, 2026
- Elucidating Heterogeneous Iron Biomineralization Patterns in a Denitrifying As(III)-Oxidizing Bacterium: Implications for Arsenic Immobilization
R. Lopez-Adams, S. M. Fairclough, … J. R. Lloyd·bioRxiv·Jan 28, 2022
- Genome mining, phylogenetic, and functional analysis of arsenic (As) resistance operons in Bacillus strains, isolated from As-rich hot spring microbial mats
A. Flores, M. F. Valencia-Marin, … G. Santoyo·bioRxiv·Mar 20, 2022
- Growth substrate limitation enhances anaerobic arsenic methylation by Paraclostridium bifermentans strain EML
J. Qiao, H. Sallet, … R. Bernier-Latmani·Applied and Environmental MicrobiologyPeer-reviewed·Dec 18, 2024
- L-Aspartate oxidase provides new insights into fumarate reduction in anaerobic darkness in Synechocystis sp. PCC6803
K. Kukil, J. A. Hawkes, … P. Lindberg·bioRxiv·Oct 19, 2022