Bioinformatic Analyses of Bacterial Mercury Ion (Hg2+) Transporters

Mok, T L; Chen, Jonathan S.; Shlykov, Maksim A.; Saier, Milton H.

doi:10.1007/s11270-012-1208-3

Cited by 10 publications

(9 citation statements)

References 25 publications

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“…It seems that the two halves of the EukAtpIs have diverged in sequence from the primordial sequence, possibly to serve distinct functions. This pathway has also been proposed in a similar study involving four TMS mercuric ion resistance channels (Mok et al, 2012) and the four TMS junctional proteins of animals (A. Lee and M. Saier, unpublished data).…”

Section: Discussionsupporting

confidence: 62%

Establishing homology between mitochondrial calcium uniporters, prokaryotic magnesium channels and chlamydial IncA proteins

2014

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Section: Discussionsupporting

confidence: 62%

Establishing homology between mitochondrial calcium uniporters, prokaryotic magnesium channels and chlamydial IncA proteins

2014

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“…These proteins have recently been shown to be fluoride export channels which protect the bacterium against the toxic effects of fluoride [51, 52]. For both the Homotrimeric Cation Channel Family (TC#1.A.62) [53] and the Mer Superfamily (TC#1.A.72) [54, 55] only L. biflexa has constituent channels. While the former proteins have not been characterized in bacteria, the latter function in the uptake of mercuric ions for the purpose of reduction to metallic mercury by a cytoplasmic mercuric reductase, a detoxification reaction [56].…”

Section: Resultsmentioning

confidence: 99%

Comparative analyses of transport proteins encoded within the genomes of Leptospira species

Buyuktimkin

Saier

2016

Microbial Pathogenesis

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Select species of the bacterial genus Leptospira are causative agents of leptospirosis, an emerging global zoonosis affecting nearly one million people worldwide annually. We examined two Leptospira pathogens, L. interrogans serovar Lai str. 56601 and L. borgpetersenii serovar Hardjo-bovis str. L550, as well as the free-living leptospiral saprophyte, L. biflexa serovar Patoc str. ‘Patoc 1 (Ames)’. The transport proteins of these leptospires were identified and compared using bioinformatics to gain an appreciation for which proteins may be related to pathogenesis and saprophytism. L. biflexa possesses a disproportionately high number of secondary carriers for metabolite uptake and environmental adaptability as well as an increased number of inorganic cation transporters providing ionic homeostasis and effective osmoregulation in a rapidly changing environment. L. interrogans and L. borgpetersenii possess far fewer transporters, but those that they all have are remarkably similar, with near-equivalent representation in most transporter families. These two Leptospira pathogens also possess intact sphingomyelinases, holins, and virulence-related outer membrane porins. These virulence-related factors, in conjunction with decreased transporter substrate versatility, indicate that pathogenicity arose in Leptospira correlating to progressively narrowing ecological niches and the emergence of a limited set of proteins responsible for host invasion. The variability of host tropism and mortality rates by infectious leptospires suggests that small differences in individual sets of proteins play important physiological and pathological roles.

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“…These proteins have recently been shown to be fluoride export channels which protect the bacterium against the toxic effects of fluoride [51, 52]. For both the Homotrimeric Cation Channel Family (TC#1.A.62) [53] and the Mercury (Mer) Superfamily (TC#1.A.72) [54, 55] only L. biflexa has constituent channels. While the former proteins have not been characterized in bacteria, the latter function in the uptake of mercuric ions for the purpose of reduction to metallic mercury by a cytoplasmic mercuric reductase, a detoxification reaction [56].…”

Section: Resultsmentioning

confidence: 99%

Comparative genomic analyses of transport proteins encoded within the genomes of Leptospira species

Buyuktimkin

Saier

2015

Microbial Pathogenesis

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Select species of the bacterial genus Leptospira are causative agents of leptospirosis, an emerging global zoonosis affecting nearly one million people worldwide annually. We examined two Leptospira pathogens, L. interrogans serovar Lai str. 56601 and L. borgpetersenii serovar Hardjo-bovis str. L550, as well as the free-living leptospiral saprophyte, L. biflexa serovar Patoc str. ‘Patoc 1 (Ames)’. The transport proteins of these leptospires were identified and compared using bioinformatics to gain an appreciation for which proteins may be related to pathogenesis and saprophytism. L. biflexa possesses a disproportionately high number of secondary carriers for metabolite uptake and environmental adaptability as well as an increased number of inorganic cation transporters providing ionic homeostasis and effective osmoregulation in a rapidly changing environment. L. interrogans and L. borgpetersenii possess far fewer transporters, but those that they have are remarkably similar, with near-equivalent representation in most transporter families. These two Leptospira pathogens also possess intact sphingomyelinases, holins, and virulence-related outer membrane porins. These virulence-related factors, in conjunction with decreased transporter substrate versatility, indicate that pathogenicity was accompanied by progressively narrowing ecological niches and the emergence of a limited set of proteins responsible for host invasion. The variability of host tropism and mortality rates by infectious leptospires suggests that small differences in individual sets of proteins play important physiological and pathological roles.

show abstract

Bioinformatic Analyses of Bacterial Mercury Ion (Hg2+) Transporters

Cited by 10 publications

References 25 publications

Establishing homology between mitochondrial calcium uniporters, prokaryotic magnesium channels and chlamydial IncA proteins

Establishing homology between mitochondrial calcium uniporters, prokaryotic magnesium channels and chlamydial IncA proteins

Comparative analyses of transport proteins encoded within the genomes of Leptospira species

Comparative genomic analyses of transport proteins encoded within the genomes of Leptospira species

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