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NarJ subfamily system specific chaperone diversity and evolution is directed by respiratory enzyme associations

Overview of attention for article published in BMC Ecology and Evolution, June 2015
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Title
NarJ subfamily system specific chaperone diversity and evolution is directed by respiratory enzyme associations
Published in
BMC Ecology and Evolution, June 2015
DOI 10.1186/s12862-015-0412-3
Pubmed ID
Authors

Denice C. Bay, Catherine S. Chan, Raymond J. Turner

Abstract

Redox 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. This 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. Examination 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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Geographical breakdown

Country Count As %
Unknown 40 100%

Demographic breakdown

Readers by professional status Count As %
Student > Bachelor 18 45%
Student > Ph. D. Student 5 13%
Researcher 4 10%
Professor 2 5%
Student > Postgraduate 2 5%
Other 5 13%
Unknown 4 10%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 24 60%
Agricultural and Biological Sciences 8 20%
Veterinary Science and Veterinary Medicine 1 3%
Medicine and Dentistry 1 3%
Chemistry 1 3%
Other 1 3%
Unknown 4 10%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 13 June 2015.
All research outputs
#22,756,649
of 25,371,288 outputs
Outputs from BMC Ecology and Evolution
#3,511
of 3,714 outputs
Outputs of similar age
#237,653
of 278,754 outputs
Outputs of similar age from BMC Ecology and Evolution
#70
of 72 outputs
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