Cloning and characterization of a gene cluster, phsBCDEF, necessary for the production of hydrogen sulfide from thiosulfate by Salmonella typhimurium

Alami, N.; Hallenbeck, Patrick C.

doi:10.1016/0378-1119(94)00930-q

Cited by 13 publications

(9 citation statements)

References 15 publications

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“…Sequencing analyses revealed that MudJ was inserted into the phsB gene of the S. enterica phsABC-dacD genetic cluster (Fig. 1D), genes that are apparently cotranscribed (13,14). phsABC genes encode the subunits of a periplasmic thiosulfate reductase involved in the dissimilatory reduction of thiosulfate to H 2 S, a pathway common to Salmonella species but rarely present among other Enterobacteriaceae members (13,14).…”

Section: Resultsmentioning

confidence: 99%

“…1D), genes that are apparently cotranscribed (13,14). phsABC genes encode the subunits of a periplasmic thiosulfate reductase involved in the dissimilatory reduction of thiosulfate to H 2 S, a pathway common to Salmonella species but rarely present among other Enterobacteriaceae members (13,14). dacD codes in turn for the LMM PBP6b, ubiquitously present in members of the Enterobacteriaceae family (15)(16)(17)(18)(19).…”

Section: Resultsmentioning

confidence: 99%

“…E. coli mutants lacking periplasmic proteins with chaperone capabilities, including SurA, FkpA, DegP, PpiA, PpiD, DsbA, DsbC, and DsbG (6, 7), showed no significant reductions in GOB-mediated CTX resistance. Yet a different approach using S. enterica MudJ transposon mutagenesis showed that an insertion in the phsABC-dacD cluster (13,14) was associated with reduced GOB-18-mediated CTX resistance. This phenotype could be associated with the deletion of the dacD gene in S. enterica and also in E. coli, concomitant with a lower accumulation of GOB-18 in the periplasm of the ⌬dacD mutants.…”

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confidence: 99%

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Low-Molecular-Mass Penicillin Binding Protein 6b (DacD) Is Required for Efficient GOB-18 Metallo-β-Lactamase Biogenesis in Salmonella enterica and Escherichia coli

Brambilla

Morán-Barrio

Viale

2014

Antimicrob Agents Chemother

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Metallo-␤-lactamases (MBLs) are Zn 2؉-containing secretory enzymes of clinical relevance, whose final folding and metal ion assembly steps in Gram-negative bacteria occur after secretion of the apo form to the periplasmic space. In the search of periplasmic factors assisting MBL biogenesis, we found that dacD null (⌬dacD) mutants of Salmonella enterica and Escherichia coli expressing the pre-GOB-18 MBL gene from plasmids showed significantly reduced resistance to cefotaxime and concomitant lower accumulation of GOB-18 in the periplasm. This reduced accumulation of GOB-18 resulted from increased accessibility to proteolytic attack in the periplasm, suggesting that the lack of DacD negatively affects the stability of secreted apo MBL forms. Moreover, ⌬dacD mutants of S. enterica and E. coli showed an altered ability to develop biofilm growth. DacD is a widely distributed low-molecular-mass (LMM) penicillin binding protein (PBP6b) endowed with low DD-carboxypeptidase activity whose functions are still obscure. Our results indicate roles for DacD in assisting biogenesis of particular secretory macromolecules in Gram-negative bacteria and represent to our knowledge the first reported phenotypes for bacterial mutants lacking this LMM PBP.␤-Lactamase production represents a common mechanism of bacterial resistance and cause of failure in the treatment of infections (1). Among the different groups of ␤-lactamases defined on the basis of structural similarity and catalytic mechanisms, the metallo-␤-lactamases (MBLs) are especially worrisome (2, 3). This group is constituted entirely of metalloenzymes employing Zn 2ϩ for catalysis; members of this group can hydrolyze a broad spectrum of substrates, including the latest generations of clinically relevant ␤-lactams, and can be rapidly spread by horizontal gene transfer (1-3). Among the different strategies for controlling MBL dissemination, efforts have so far been focused on the design of a general MBL inhibitor, a goal so far hindered by the diversity of active-site structures among these metalloenzymes (4).A less known aspect of MBL research, but one that may provide potential targets for antimicrobial drug design, is the MBL biogenesis pathway (5). We previously reported that the productive biogenesis of the GOB-18 MBL in Escherichia coli requires an "expanded" DnaK chaperone system to assist the cytoplasmic transit of the preapoprotein to the secretion system (5). Moreover, we also found that secretion of the apo GOB-18 form is driven by the Sec (SecA-SecYEG) machinery, implying that final folding and Zn 2ϩ ion assembly to the native MBL conformation occur in the periplasm (5). Unfolded proteins emerging from the Sec channel are greeted by a highly complex macromolecule-crowded environment containing an array of modifying enzymes, some of them endowed with the ability to act as folding assistants (6-8). This complex scenario can certainly affect individual folding landscapes (6), but whether the final steps of MBL folding and Zn 2ϩ assembly are assisted by periplasmic ...

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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confidence: 99%

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Low-Molecular-Mass Penicillin Binding Protein 6b (DacD) Is Required for Efficient GOB-18 Metallo-β-Lactamase Biogenesis in Salmonella enterica and Escherichia coli

Brambilla

Morán-Barrio

Viale

2014

Antimicrob Agents Chemother

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“…Porwollik et al (2002) identified a set of genes specific for S. enterica compared to two E. coli strains (K12 and O157:H7), Klebsiella pneumoniae MGH 78578, and Yersinia pestis CO92 (59). This set included CDS from the ttr, phs, and asr operons involved in the dissimilatory reduction of oxidized sulfur compounds under anaerobic conditions (2,15,31,37). Since CDS of these operons were found to be absent from several S. enterica genomes analyzed by BLAST score ratio in this study, the presence of a larger group of CDS involved in anaerobic respiration was examined across all sequenced genomes (see Table S3 in the supplemental material).…”

Section: ) (33)mentioning

confidence: 99%

Comparative Genomics of 28 Salmonella enterica Isolates: Evidence for CRISPR-Mediated Adaptive Sublineage Evolution

et al. 2011

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Despite extensive surveillance, food-borne Salmonella enterica infections continue to be a significant burden on public health systems worldwide. As the S. enterica species comprises sublineages that differ greatly in antigenic representation, virulence, and antimicrobial resistance phenotypes, a better understanding of the species' evolution is critical for the prediction and prevention of future outbreaks. The roles that virulence and resistance phenotype acquisition, exchange, and loss play in the evolution of S. enterica sublineages, which to a certain extent are represented by serotypes, remains mostly uncharacterized. Here, we compare 17 newly sequenced and phenotypically characterized nontyphoidal S. enterica strains to 11 previously sequenced S. enterica genomes to carry out the most comprehensive comparative analysis of this species so far. These phenotypic and genotypic data comparisons in the phylogenetic species context suggest that the evolution of known S. enterica sublineages is mediated mostly by two mechanisms, (i) the loss of coding sequences with known metabolic functions, which leads to functional reduction, and (ii) the acquisition of horizontally transferred phage and plasmid DNA, which provides virulence and resistance functions and leads to increasing specialization. Matches between S. enterica clustered regularly interspaced short palindromic repeats (CRISPR), part of a defense mechanism against invading plasmid and phage DNA, and plasmid and prophage regions suggest that CRISPR-mediated immunity could control short-term phenotype changes and mediate long-term sublineage evolution. CRISPR analysis could therefore be critical in assessing the evolutionary potential of S. enterica sublineages and aid in the prediction and prevention of future S. enterica outbreaks.

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“…2 and Table 2; see also (36), and sulfur reductase (SreABC) from A. ambivalens (31). This family of proteins is mostly found in anaerobic bacteria although anoxic conditions appear to be required for transcriptional regulation but not activity (1,20). Members of this family are heterotrimers in which the catalytic ␣ and ␤ subunits are both hydrophilic and contain 4Fe-4S and/or 3Fe-4S coordination sites (as recognized by characteristic Cys-rich motifs).…”

Section: New Components Of Fe(ii)-induced Electron Transport Chainsmentioning

confidence: 99%

Identification of Components of Electron Transport Chains in the Extremely Thermoacidophilic Crenarchaeon Metallosphaera sedula through Iron and Sulfur Compound Oxidation Transcriptomes

Auernik

Kelly

2008

Appl Environ Microbiol

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The crenarchaeal order Sulfolobales collectively contain at least five major terminal oxidase complexes. Based on genome sequence information, all five complexes are found only in Metallosphaera sedula and Sulfolobus tokodaii, the two sequenced Sulfolobales capable of iron oxidization. While specific respiratory complexes in certain Sulfolobales have been characterized previously as proton pumps for maintaining intracellular pH and generating proton motive force, their contribution to sulfur and iron biooxidation has not been considered. For M. sedula growing in the presence of ferrous iron and reduced inorganic sulfur compounds (RISCs), global transcriptional analysis was used to track the response of specific genes associated with these complexes, as well as other known and putative respiratory electron transport chain elements. Open reading frames from all five terminal oxidase or bc 1 -like complexes were stimulated on one or more conditions tested. Components of the fox (Msed0467 to Msed0489) and soxNL-cbsABA (Msed0500 to Msed0505) terminal/quinol oxidase clusters were triggered by ferrous iron, while the soxABCDD terminal oxidase cluster (Msed0285 to Msed0291) were induced by tetrathionate and S 0 . Chemolithotrophic electron transport elements, including a putative tetrathionate hydrolase (Msed0804), a novel polysulfide/sulfur/dimethyl sulfoxide reductase-like complex (Msed0812 to Msed0818), and a novel heterodisulfide reductase-like complex (Msed1542 to Msed1550), were also stimulated by RISCs. Furthermore, several hypothetical proteins were found to have strong responses to ferrous iron or RISCs, suggesting additional candidates in iron or sulfur oxidation-related pathways. From this analysis, a comprehensive model for electron transport in M. sedula could be proposed as the basis for examining specific details of iron and sulfur oxidation in this bioleaching archaeon.Certain extremely thermoacidophilic archaea are promising candidates for biomining operations targeting the recovery of base and precious metals (44). These microorganisms grow at elevated temperatures where abiotic ferrous oxidation rates are accelerated and where passivation of mineral surfaces from reduced inorganic sulfur compounds (RISCs) is minimal (44). To tap into the biotechnological potential of these microorganisms, their physiological characteristics that relate to metal mobilization need to be better understood, especially mechanisms underlying biooxidation of iron (Fe 2ϩ ) and RISCs. Biooxidation implicates membrane-associated protein complexes that mediate electron transport, which seemingly determines the capability and capacity of extreme thermoacidophiles for metal and sulfur mobilization. However, the complexes required for bioleaching have not been established. Models that address the specific and collective function of electron transport complexes in the Sulfolobales are needed to provide a physiological framework for exploring the intricacies of biological metal and sulfur oxidation.Current knowledge of respiratory el...

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Cloning and characterization of a gene cluster, phsBCDEF, necessary for the production of hydrogen sulfide from thiosulfate by Salmonella typhimurium

Cited by 13 publications

References 15 publications

Low-Molecular-Mass Penicillin Binding Protein 6b (DacD) Is Required for Efficient GOB-18 Metallo-β-Lactamase Biogenesis in Salmonella enterica and Escherichia coli

Low-Molecular-Mass Penicillin Binding Protein 6b (DacD) Is Required for Efficient GOB-18 Metallo-β-Lactamase Biogenesis in Salmonella enterica and Escherichia coli

Comparative Genomics of 28 Salmonella enterica Isolates: Evidence for CRISPR-Mediated Adaptive Sublineage Evolution

Identification of Components of Electron Transport Chains in the Extremely Thermoacidophilic Crenarchaeon Metallosphaera sedula through Iron and Sulfur Compound Oxidation Transcriptomes

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