ArticleBMC evolutionary biology2015
NarJ subfamily system specific chaperone diversity and evolution is directed by respiratory enzyme associations.
Article in BMC evolutionary biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 15 citations in OpenAlex.
- Sulfur disproportionation occurs globally across anoxic habitats and has multiple mechanisms of independent evolutionary origin.The ISME journal · 2026Review
- Structural analysis of YcdY, a member of the redox-enzyme maturation protein family.Acta crystallographica. Section F, Structural biology communications · 2025Article
- History of Maturation of Prokaryotic Molybdoenzymes-A Personal View.Molecules (Basel, Switzerland) · 2023Review
- Antibiotic Resistance Diagnosis in ESKAPE Pathogens-A Review on Proteomic Perspective.Diagnostics (Basel, Switzerland) · 2023Review
- Molecular Characteristics and Quantitative Proteomic Analysis ofAntibiotics (Basel, Switzerland) · 2022Article
- Influence of the TorD signal peptide chaperone on Tat-dependent protein translocation.PloS one · 2021Article
- A dual functional redox enzyme maturation protein for respiratory and assimilatory nitrate reductases in bacteria.Molecular microbiology · 2019Article
- A phylogenomic and ecological analysis of the globally abundant Marine Group II archaea (Ca. Poseidoniales ord. nov.).The ISME journal · 2019Article
- A new family of periplasmic-binding proteins that sense arsenic oxyanions.Scientific reports · 2018Article
- Same but different: Comparison of two system-specific molecular chaperones for the maturation of formate dehydrogenases.PloS one · 2018Article
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3 authors at 1 institution in 1 country.
Funding
Abstract
backgroundRedox enzyme maturation proteins (REMPs) describe a diverse family of prokaryotic chaperones involved in the biogenesis of anaerobic complex iron sulfur molybdoenzyme (CISM) respiratory systems. Many REMP family studies have focused on NarJ subfamily members from Escherichia coli: NarJ, NarW, DmsD, TorD and YcdY. The aim of this bioinformatics study was to expand upon the evolution, distribution and genetic association of these 5 REMP members within 130 genome sequenced taxonomically diverse species representing 324 Prokaryotic sequences. NarJ subfamily member diversity was examined at the phylum-species level and at the amino acid/nucleotide level to determine how close their genetic associations were between their respective CISM systems within phyla.
resultsThis study revealed that NarJ members possessed unique motifs that distinguished Gram-negative from Gram-positive/Archaeal species and identified a strict genetic association with its nitrate reductase complex (narGHI) operon compared to all other members. NarW appears to be found specifically in Gammaproteobacteria. DmsD also showed close associations with the dimethylsulfoxide reductase (dmsABC) operon compared to TorD. Phylogenetic analysis revealed that YcdY has recently evolved from DmsD and that YcdY has likely diverged into 2 subfamilies linked to Zn- dependent alkaline phosphatase (ycdX) operons and a newly identified operon containing part of Zn-metallopeptidase FtsH complex component (hflC) and NADH-quinone dehydrogenase (mdaB). TorD demonstrated the greatest diversity in operon association. TorD was identifed within operons from either trimethylamine-N-oxide reductase (torAC) or formate dehydrogenase (fdhGHI), where each type of TorD had a unique motif. Additionally a subgroup of dmsD and torD members were also linked to operons with biotin sulfoxide (bisC) and polysulfide reductase (nrfD) indicating a potential role in the maturation of diverse CISM.
conclusionExamination of diverse prokaryotic NarJ subfamily members demonstrates that the evolution and genetic association of each member is uniquely biased by its CISM operon association.
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