Molecular characterization of LhpR in control of hydroxyproline catabolism and transport in Pseudomonas aeruginosa PAO1

Li, Guoqing; Lu, Chung‐Dar

doi:10.1099/mic.0.000300

Cited by 12 publications

(19 citation statements)

References 27 publications

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“…In addition, during colonization P. aeruginosa can degrade collagen molecules via the secretion of elastase and alkaline protease AprA (Bejarano et al, 1989 ). The collagen breakdown releases large amounts of the modified amino acid hydroxyproline (Hyp) (Gorres and Raines, 2010 ), which can be further catabolized by P. aeruginosa lhp genes (Li and Lu, 2016 ). Analysis of BWE composition revealed a higher Hyp concentration than in burn patient plasma, consistent with a possible Hyp release at the burn wound site caused by basal lamina destruction (Figure 5B ).…”

Section: Resultsmentioning

confidence: 99%

Transcriptome Analysis of Pseudomonas aeruginosa Cultured in Human Burn Wound Exudates

Gonzalez

Ducret

Leoni

et al. 2018

Front. Cell. Infect. Microbiol.

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Pseudomonas aeruginosa is a severe opportunistic pathogen and is one of the major causes of hard to treat burn wound infections. Herein we have used an RNA-seq transcriptomic approach to study the behavior of P. aeruginosa PAO1 growing directly on human burn wound exudate. A chemical analysis of compounds used by this bacterium, coupled with kinetics expression of central genes has allowed us to obtain a global view of P. aeruginosa physiological and metabolic changes occurring while growing on human burn wound exudate. In addition to the numerous virulence factors and their secretion systems, we have found that all iron acquisition mechanisms were overexpressed. Deletion and complementation with pyoverdine demonstrated that iron availability was a major limiting factor in burn wound exudate. The quorum sensing systems, known to be important for the virulence of P. aeruginosa, although moderately induced, were activated even at low cell density. Analysis of bacterial metabolism emphasized importance of lactate, lipid and collagen degradation pathways. Overall, this work allowed to designate, for the first time, a global view of P. aeruginosa characteristics while growing in human burn wound exudate and highlight the possible therapeutic approaches to combat P. aeruginosa burn wound infections.

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Section: Resultsmentioning

confidence: 99%

Transcriptome Analysis of Pseudomonas aeruginosa Cultured in Human Burn Wound Exudates

Gonzalez

Ducret

Leoni

et al. 2018

Front. Cell. Infect. Microbiol.

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“…1d)28. Among the 18 components, 10 genes including PA1259 ( LhpI ) were significantly induced by trans -4-hydroxy-L-proline.…”

Section: Resultsmentioning

confidence: 99%

“…Furthermore, the LhpI mutant, constructed by transposon insertion, as well as mutants of the known trans -4-hydroxy-L-proline metabolic gene lost the ability to grow on trans -4-hydroxy-L-proline. However, this phenotype may be due to a polar effect on downstream genes28. The non-polar LhpI deletion mutant (SMb20269; Fig.…”

Section: Resultsmentioning

confidence: 99%

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Functional characterization of aconitase X as a cis-3-hydroxy-L-proline dehydratase

Watanabe

Tajima

Fujii

et al. 2016

Sci Rep

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In the aconitase superfamily, which includes the archetypical aconitase, homoaconitase, and isopropylmalate isomerase, only aconitase X is not functionally annotated. The corresponding gene (LhpI) was often located within the bacterial gene cluster involved in L-hydroxyproline metabolism. Screening of a library of (hydroxy)proline analogues revealed that this protein catalyzes the dehydration of cis-3-hydroxy-L-proline to Δ1-pyrroline-2-carboxylate. Furthermore, electron paramagnetic resonance and site-directed mutagenic analyses suggests the presence of a mononuclear Fe(III) center, which may be coordinated with one glutamate and two cysteine residues. These properties were significantly different from those of other aconitase members, which catalyze the isomerization of α- to β-hydroxy acids, and have a [4Fe-4S] cluster-binding site composed of three cysteine residues. Bacteria with the LhpI gene could degrade cis-3-hydroxy-L-proline as the sole carbon source, and LhpI transcription was up-regulated not only by cis-3-hydroxy-L-proline, but also by several isomeric 3- and 4-hydroxyprolines.

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“…The genes hypA to hypK often cluster together with the putative L-Hyp (ABC-type) transporter genes (22), the transcriptional regulator gene (13,23), the enolase-like gene (hypJ) (24), the aconitase X-like gene (hypI), and the proline racemase-like gene (hypL) on bacterial genomes (Fig. 2D).…”

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confidence: 99%

Characterization of a Novel cis -3-Hydroxy- l -Proline Dehydratase and a trans -3-Hydroxy- l -Proline Dehydratase from Bacteria

et al. 2017

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Hydroxyprolines, such as trans-4-hydroxy-L-proline (T4LHyp), trans-3-hydroxy-L-proline (T3LHyp), and cis-3-hydroxy-L-proline (C3LHyp), are present in some proteins including collagen, plant cell wall, and several peptide antibiotics. In bacteria, genes involved in the degradation of hydroxyproline are often clustered on the genome (L-Hyp gene cluster). We recently reported that an aconitase X (AcnX)-like hypI gene from an L-Hyp gene cluster functions as a monomeric C3LHyp dehydratase (AcnX Type I ). However, the physiological role of C3LHyp dehydratase remained unclear. We here demonstrate that Azospirillum brasilense NBRC 102289, an aerobic nitrogen-fixing bacterium, robustly grows using not only T4LHyp and T3LHyp but also C3LHyp as the sole carbon source. The small and large subunits of the hypI gene (hypI S and hypI L , respectively) from A. brasilense NBRC 102289 are located separately from the L-Hyp gene cluster and encode a C3LHyp dehydratase with a novel heterodimeric structure (AcnX Type IIa ). A strain disrupted in the hypI S gene did not grow on C3LHyp, suggesting its involvement in C3LHyp metabolism. Furthermore, C3LHyp induced transcription of not only the hypI genes but also the hypK gene encoding Δ 1 -pyrroline-2-carboxylate reductase, which is involved in T3LHyp, D-proline, and D-lysine metabolism. On the other hand, the L-Hyp gene cluster of some other bacteria contained not only the AcnX Type IIa gene but also two putative proline racemase-like genes (hypA1 and hypA2). Despite having the same active sites (a pair of Cys/Cys) as hydroxyproline 2-epimerase, which is involved in the metabolism of T4LHyp, the dominant reaction by HypA2 was clearly the dehydration of T3LHyp, a novel type of T3LHyp dehydratase that differed from the known enzyme (Cys/Thr). L-hydroxyproline) degradation in aerobic bacteria, its genetic and molecular information has only recently been elucidated. L-Hydroxyproline metabolic genes are often clustered on bacterial genomes. These loci frequently contain a hypothetical gene(s), whose novel enzyme functions are related to the metabolism of trans-3-hydroxyL-proline and/or cis-3-hydroxyL-proline, a relatively rare L-hydroxyproline in nature. Several L-hydroxyproline metabolic enzymes show no sequential similarities, suggesting their emergence by convergent evolution. Furthermore, transcriptional regulation by trans-4-hydroxy-L-proline, trans-3-hydroxy-L-proline, and/or cis-3-hydroxy-L-proline significantly differs between bacteria. The results of the present study show that several L-hydroxyprolines are available for bacteria as carbon and energy sources and may contribute to the discovery of potential metabolic pathways of another hydroxyproline(s). IMPORTANCE More than 50 years after the discovery of trans-4-hydroxy-L-proline (generally calledKEYWORDS aconitase X, proline racemase superfamily, gene cluster, hydroxyproline, convergent evolution

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Molecular characterization of LhpR in control of hydroxyproline catabolism and transport in Pseudomonas aeruginosa PAO1

Cited by 12 publications

References 27 publications

Transcriptome Analysis of Pseudomonas aeruginosa Cultured in Human Burn Wound Exudates

Transcriptome Analysis of Pseudomonas aeruginosa Cultured in Human Burn Wound Exudates

Functional characterization of aconitase X as a cis-3-hydroxy-L-proline dehydratase

Characterization of a Novel cis -3-Hydroxy- l -Proline Dehydratase and a trans -3-Hydroxy- l -Proline Dehydratase from Bacteria

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