- Volume 144, Issue 10, 1998
Volume 144, Issue 10, 1998
- Review Article
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- Bioenergetics And Transport
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The Nhal antiporter of Saccharomyces cerevisiae mediates sodium and potassium eft: lux
More LessSUMMARY: The NHAl gene of Saccharomyces cerevisiae, transcribed into a 3-5 kb mRNA, encodes a protein mediating Na+ and K+ efflux through the plasma membrane that is required for alkali cation tolerance at acidic pH. Deletion of the gene in a wild-type strain resulted in higher sensitivity to both K+ and Na+ at acidic pH. Measurements of cation loss in strains carrying deleted or overexpressed alleles of NHAl demonstrated its role in K+ and Na+ efflux. In addition, high K+ and Na+ efflux observed upon alkalinization of the cytoplasm implies a role of Nhalp in the regulation of intracellular pH. Moreover, the overexpression of ENA1 and NHAl genes in an enal-46-nhalb strain showed that the Nhal alkalication antiporter is responsible for growth on high concentrations of KCI and NaCl at acidic pH, and Ena alkali-cation ATPases are necessary at higher pH values. Both systems have a complementary action to maintain the intracellular steadystate concentration of K+ and Na+.
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Transmembrane topology of the two FhuB domains representing the hydrophobic components of bacterial ABC transporters involved in the uptake of siderophores, haem and vitamin B
More LessSUMMARY: Transport of siderophores of the hydroxamate type across the Escherichia coli cytoplasmic membrane depends on a periplasmic binding-protein-dependent (PBT) system. This uptake system consists of the binding protein FhUD, the membrane-associated putative ATP-hydrolase FhuC and the integral membrane protein FhuB. The two halves of FhuB [FhuB(N) and FhuB(C)], both essential for transport, are similar with respect to structure and function. Regions were identified in FhuB(N) and FhuB(C) which are presumably involved in the interaction of the two FhuB halves with each other or with other components of the uptake system, or with the different substrates. To determine the topology of the membrane-embedded polypeptide chain, FhuB‘-’/?-lactamase protein fusions were analysed. The experimental data suggest that each half of the FhuB is able to fold autonomously into the lipid bilayer, which is a prerequisite for the assembly of both halves into a transport-competent formation. The hydrophobic components from PBT systems involved in the uptake of siderophores, haem and vitamin B, define a subclass of polytopic integral membrane proteins. The topology of these ‘siderophore family’ proteins differs from that of the equivalent components of other PBT systems in that each polypeptide (and each half of FhuB) consists of 10 membrane- spanning regions, with the N- and C-termini located in the cytoplasm. The conserved region at a distance of about 90 amino acids from the C-terminus, typical of all hydrophobic PBT proteins, is also oriented to the cytoplasm. However, in the siderophore family’ proteins this putative ATPase interaction loop is followed by four instead of two transmembrane spans.
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- Environmental Microbiology
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In situ detection of bacteria in continuous-flow cultures of seawater sediment suspensions with f luorescently labelled rRNA-directed oligonucleotide probes
More LessSUMMARY: RNA-targeted and f luorescently labelled oligonucleotide probes were used to study the composition of natural bacterial populations in continuous-f low cultures of seawater sediment suspensions. The cultures were run as enrichment cultures with increasing dilution rates, and hexadecane as the sole carbon source. Total cell numbers were analysed by counting DAPI (4′,6- diamidino-2-phenylindole)-stained cells. To differentiate the population composition, oligonucleotide probes for eubacteria, for Cytophagd Flavobacteria, and for four subclasses of the Proteobacteria (a, b, y and 6) were used. About 4&80°/o of the DAPI-stained cells could be detected with the EUB338 probe. Moreover, it was possible to detect a shift in the composition of the natural bacterial population with increasing dilution rate of the continuous culture, from large amounts of CytophagdFlavobacteria to large numbers of members of the pProteobacteria. The cell recovery rate for bacteria labelled with specific oligonucleotide probes was analysed with defined cell numbers of Rhodospirillum nrbnrm, Cornamonas testosteroni and Desulfowibrio vulgaris subsp. vulgaris introduced into the seawater sediment suspension, and was determined to be 13*%33*5 %. The standard deviation determined for this method applied to sediment suspensions was 28.3 %. The results suggest that the application of the in situ hybridization technique allows a good insight into the structure of populations growing in sediment suspensions.
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- Genetics And Molecular Biology
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The mabA gene from the inhA operon of Mycobacterium tuberculosis encodes a 3lketoacyl reductase that fails to confer isoniazid resistance
More LessSUMMARY: A target of the anti-tuberculosis drugs isoniazid (INH) and ethionamide (ETH) has been shown to be an enoyl reductase, encoded by the inhA gene. The mabA (mycolic acid biosynthesis A) gene is located immediately upstream of inhA in Mycobacterium tuberculosis, Mycobacterium bo wis and Mycobacterium smegmatis. The MabA protein from M. tuberculosis was expressed in Escherichia coli and shown to have 3-ketoacyl reductase activity, consistent with a role in mycolic acid biosynthesis. In M. smegmatis, inhA and mabA are independently transcribed, but in M. tuberculosis and M. bowis BCG, mabA and inhA constitute a single operon. Several INH-ETH-resistant M. tuberculosis clinical isolates contain point mutations in the ribosome-binding site of mabA in the mabA-inhA operon. However, genetic dissection of this operon reveals that the INH-ETH-resistance phenotype is encoded only by hhA, and not by mabA.
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A chromosomal ars operon homologue of Pseudomonas aeruginosa confers increased resistance to arsenic and antimony in Escherichia coli
More LessSUMMARY: Operons encoding homologous arsenic-resistance determinants (ars) have been discovered in bacterial plasmids from Gram-positive and Gram-negative, organisms, as well as in the Escherichia coli chromosome. However, evidence for this arsenic-resistance determinant in the medically and environmentally important bacterial species Pseudomonas aeruginosa is conflicting. Here the identification of a P. aeruginosa chromosomal ars operon homologue via cloning and complementation of an E. coli ars mutant is reported. The P. aeruginosa chromosomal ars operon contains three potential ORFs encoding proteins with significant sequence similarity to those encoded by the arsR, arsB and arsC genes of the plasmid-based and E. coli chromosomal ars operons. The cloned P. aeruginosa chromosomal ars operon confers augmented resistance to arsenic and antimony oxyanions in an E. coli arsB mutant and in wild-type P. aeruginosa. Expression of the operon was induced by arsenite at the mRNA level. DNA sequences homologous with this operon were detected in some, but not all, species of the genus Pseudomonas, suggesting that its conservation follows their taxonomic-based evolution.
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Differential regulation of SAP8 and SAPS, which encode two new members of the secreted aspartic proteinase family in Candida albicans
More LessSUMMARY: Secreted aspartic proteinases (Saps) contribute to the virulence of Candida albicans in systemic animal models of infection. Seven genes encoding Saps (SAM-SAP7) have been identified to date but evidence suggested the existence of additional SAP genes. The screening of a C. albicans iZEMBL3 genomic library for the presence of other SAP genes was undertaken. Two new genes, SAP8 and SAPS, were isolated. The N-terminal amino acid sequence deduced from SAP8 downstream of a Kex2plike cleavage site corresponds to the N-terminal amino acid sequence of the 41 kDa Sap isolated and characterized previously. SAP8 mRNA was expressed preferentially in yeasts at 25 "C after 6 and 9 h growth in BSA-containing medium. SAPS encodes an aspartic proteinase with a Kex2pllike cleavage site and contains a putative glycophosphatidylinositol-anchor signal at the C-terminus. Although the SAPS gene product has not yet been isolated from cultures of C. albicans, transcripts of SAPS were observed preferentially in later growth phases when SAP8 expression had decreased.
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The conjugative plasmid pSG5 from Streptomyces ghanaensis DSM 2932 differs in its transfer functions from other Streptomyces rolling-circle-type plasmids
More LessSUMMARY: The Streptomyces ghanaensis plasmid pSG5 is self-transmissible but does not form the growth-retardation zones (pocks) normally characteristic of the Streptomyces plasmid-transfer process. The complete nucleotide sequence of pSG5 was determined on both strands. pSG5 is 12208 bp in length and has a GC content of 68 mol0/o. Characterization’ of the open reading frames by insertion and deletion analysis revealed that only a single gene, traB, is involved in the transfer of pSG5. The deduced amino acid sequence of TraB is similar to the SpolllE protein that is responsible for chromosome translocation during prespore formation of Bacillus subtilis. In contrast to the tra genes of the other Streptomyces plasmids, the pSG5 traB does not represent a kill function. Although pSG5 transfer is not associated with pock formation, pSG5 was shown to possess putative spd genes that are responsible for the pock phenotype of other Streptomyces plasmids. However, promoter-probe experiments revealed that the spd genes of pSG5 are not transcribed, thus explaining the deficiency in pock formation.
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Identification of two linear plasmids in the actinomycete Planobispora rosea
More LessSUMMARY: Two linear plasmids (pPR1, 27.5 kb, and pPR2, 16 kb) were identified in Planobispora msea, an actinomycete that produces the antibiotic GE2270, an inhibitor of the elongation factor Tu. Strains lacking both plasmids still produce and are resistant to GE2270. The two plasmids share an internal region of high similarity, but no cross-hybridization was detected between their telomeric regions or between plasmid and chromosomal DNA. The 5‵ ends of the plasmids appear to be linked to terminal proteins. The telomeric regions of pPR2 were cloned after 3‵-end homopolymer tailing and PCR amplification. The approximately 650 nt telomeric DNA sequences of pPR2 are repeated in inverted orientation and are rich in direct and inverted repeats; the 350 bp terminal region is less G+C-rich than the rest of the plasmid. The structural organization of these plasmids appears to be similar to Streptomyces linear rep1icons.
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pBLA8, from Brevibacterium linens, belongs to a Gram-positive subfamily of ColE2-related plasmids
More LessSUMMARY: A 3.1 kb DNA fragment from pBLA8, a Brevibacterium linens cryptic plasmid, containing all the information required for autonomous replication was cloned and sequenced. Using deletion analysis, the fragment essential and sufficient for autonomous replication was delimited to 1.5 kb. This fragment is characterized by the presence of an ori site located upstream of an operon encoding two proteins, RepA and RepB, both essential for replication. Based on structural similarities and a strong conservation of ori, RepA and RepB, pBLA8 was assigned to a new subfamily of the ColE2 plasmid family. This subfamily is distinguished by the requirement for two Rep proteins and the location of an ori site upstream of the mpAB operon. RepA is thought to encode primase activity, whereas RepB could be a DNA-binding protein. An Escherichia coli-B. linens shuttle vector, derived from pBLA8, was constructed. Its host spectrum was extended to Arthrobacter species.
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Divercin V41, a new bacteriocin with two disulphide bonds produced by Carnobacterium divergens V41: primary structure and genomic organization
SUMMARY: Divercin V41 is a new bacteriocin produced by Carnobacterium divergens V41, a lactic acid bacterium isolated from fish viscera. The amino acid sequence of divercin V41 showed high homologies with pediocin PA-1 and enterocin A. Two disulphide bonds were present in the hydrophilic N-terminal domain and in the highly variable hydrophobic C-terminal domain, respectively. A DNA probe designed from the N-terminal sequence of the purified peptide was used to locate the structural gene of divercin V41. A 6 kb chromosomal fragment containing the divercin V41 structural gene (dvnA) was cloned and sequenced. The results indicate that divercin V41 is synthesized as a pre-bacteriocin of 66 amino acids. The 23-residue N-terminal extension is cleaved off t o yield the mature 43-amino-acid divercin V41. In addition, the fragment encodes putative proteins commonly found within bacteriocin operons, including an ATP- dependent transporter, two immunity-like proteins and the two components of a lantibiotic-type signal-transducing system. The genetic organization of the fragment suggested important gene rearrangements.
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Heterologous expression of the bacteriocin mesentericin Y105 using the dedicated transport system and the general secretion pathway
More LessSUMMARY: Two different N-terminal extensions have been identified within class II bacteriocin precursors. The first one is a two-glycine-type leader peptide associated with a dedicated ATP-binding cassette transporter. The second is a signal peptide which directs the bacteriocin precursor to the general secretion machinery. Mesentericin Y105 is a class II anti-Listeria bacteriocin produced by Leuconostoc mesentemides Y105 via a dedicated transport system (DTS). To investigate heterologous expression systems capable of producing mesentericin Y105 in various hosts, two different secretion vectors were constructed. One of them, containing the mesentericin Y105 structural gene fused to the segment encoding the divergicin A signal peptide, was introduced into Escherichia coli, Leuconostoc subsp. and Lactococcus subsp. In E. coli, mesentericin Y105 production was linked to a putative periplasmic toxicity. To take advantage of this secretion system, the mesentericin Y105 precursor was also produced in E. coli. It was demonstrated that this pre-bacteriocin exhibited some antagonistic activity against Listeria. To allow for comparison between the two different transport systems, mesentericin Y105 production using the vector containing the mesentericin Y105 structural genem and i t s DTS transporter operon was examined. The production of mesentericin Y105 was monitored by a new fast purification method followed by MS analysis. It was shown that, in Leuconostoc, the production of mesentericin Y105 is enhanced via the DTS compared to the general secretion pathway.
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Selection and characterization of mercury- independent activation mutants of the Tn501 transcriptional regulator, MerR
More LessSUMMARY: MerR is the transcriptional regulator of the mercury-resistance (mer) operon of transposon TnSO1, acting at the mer promoter as both an activator in the presence of mercuric salts and a repressor in their absence. This paper reports a method for selection of constitutive activator mutants, which activate transcription in the absence of Hg", and the characterization of these MerRAC proteins. At least two mutations in the MerR protein were found necessary for strong mercury-independent activation, and these mutations lie in the C- terminal two-thirds of the MerR protein near the Hg"-binding cysteines. Anm triple mutation was shown t o increase activation over the corresponding double mutations. All mutant proteins caused further activation in the presence of Hg". The data support a mechanism in which a conformational change of one or both MerR subunits in the homodimer drives a distortion of DNA bound t o a helix-turn-helix structure in the N-terminal region. A mutation in this putative helix-turn-helix region severely reduced both the repressor and activator functions of MerR.
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Roles for GcvA-binding sites 3 and 2 and the Lrp-binding region in gcvT:: lacZ expression in Escherichia coli
More LessSUMMARY: GcvA and Lrp are both necessary for activation of the gcv operon. The upstream GcvA-binding sites 3 and 2 were separated from the Lrplbinding region and the rest of the gcv control region. Moving these sites by 1 or 2 helical turns of DNA further from the gcv promoter reduces, but does not eliminate, either GcvA-mediated activation or repression of a gcvT:: lac2 gene fusion. However, moving these sites by 1-5 or 2.5 helical turns of DNA results inm a GcvA-mediated super-repression of the operon. This repression is dependent on Lrp and is partially dependent on GcvR. Lrp bound to the gcv control region induces a bend in the DNA. Based on these results, a model for gcw regulation is presented in which Lrp plays a primarily structural role, by bending the DNA and GcvA functions as the activator protein.
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Two-component signal-transducing systems involved in stress responses and vancomycin susceptibility in Lactobacillus sakei
More LessSUMMARY: Fragments of five rrp genes encoding response regulators (RRs) in LactobscMus sakei were amplified by PCR using degenerate oligonucleotide primers. The five rrp genes were part of distinct loci that also comprised hpk genes encoding histidine protein kinases (HPKs). The putative RRs belonged tom the OmpR-PhoB subclass of response regulators that consist of N-terminal receiver and C-terminal DNA-binding domains. The putative HPKs were members of the EnvZ-NarX family of orthodox histidine protein kinases which possess two transmembrane segments in a non-conserved N-terminal domain and a C-terminal cytoplasmic kinase domain. Insertional inactivation of the rrp genes indicated that the RRs are implicated in susceptibility to the glycopeptide antibiotic vancomycin, and to extreme pH, temperature and oxidative conditions.
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Clustered organization and transcriptional analysis of a family of five csp genes of Lactococcus /actis MGl363
More LessSUMMARY: A family of genes encoding cold-shock proteins, named cspA, cspB, cspC, cspD and cspE, was cloned and sequenced from Lactococcus lactis MG1363. The genes cspA and cspB and the genes cspC and cspD are located in tandem repeats, an organization of csp genes that has never been encountered before. The five genes encode small (7.1-706 kDa) proteins with high mutual sequence identities (up to 85 O/O) and high identities (about 45-65 %) with the major cold- shock proteins from Escherichia coli (CspA) and Bacillus subtilis (CspB)., Northern-blot analysis revealed single transcripts of about 300 nucleotides for each csp gene and showed that cspA, cspB, cspC and cspD mRNA levels were strongly increased upon cold shock to 10 "C (about lo-, 40-, 10- and 30-fold compared to 30 "C, respectively), whereas the cspE mRNA level was not increased. The expression of the cold-induced csp genes was highest in the. 6-8 h lag phase after cold shock. A differential expression in time, in which cspA and cspC were maximally expressed at 2 h and cspB and cspD at 4 h after cold shock, was observed. The -35 and -10 regions of the five promoters were identified and transcriptional start sites were mapped in each case by primer extension at different temperatures which confirmed that regulation takes place at the transcriptional level. Significant differences were observed between the 5′-untranslated leader regions of the four cold-induced csp genes and the corresponding region of the non-cold-induced cspE gene.
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Adaptation of Cornamonas testosteroni TAM1 to utilize phenol: organization and regulation of the genes involved in phenol degradatio
More LessSUMMARY: Comamonas testosteroni TAU1 was not able to grow on phenol as a sole carbon and energy source, but it gained the ability to utilize phenol after a 2-3-week incubation in a medium containing phenol. Phenol hydroxylase (PH) and catechol2,3-dioxygenase (C230) were highly induced by phenol in the adapted strain designated as strain P1, suggesting that phenol was degraded via the meta-pathway. Gene clusters for phenol degradation were isolated from both strains TAU1 and P1. The structural genes encoding multi- component PH and C230 (aphKLMNOPQB), and a regulatory gene of the NtrC family (aphR), were located in a divergent transcriptional organization. The cloned aphKLMNOPQl3 genes from either strain TAU1 or strain P1 produced active PH and C230 enzymes in strain TA441. No difference was found between the strains in the sequences of aphR and the intergenic promoter region of aphK and aphR. However, the transcriptional activities of the aphK and aphR promoters were higher in strain P1 than in strain TA441. The aphK-promoter activity was not observed in aphR mutant strains and these strains could not grow on phenol. The aphR mutant of strain P1 was able to grow on phenol after transformation with a recombinant aphR gene but strain TAM1 was not, suggesting that the expression of the aph genes is silenced by an unidentified repressor in strain TAU1 and that this repressor is modified in strain P1.
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The localization of KpsC, S and T, and KfiA, C and D proteins involved in the biosynthesis of the Escherichia coli K5 capsular polysaccharide: evidence for a membrane-bound complex
More LessSUMMARY: Biosynthesis of the Escherichis coli K5 polysaccharide requires the Kf iA, Kf iB, KfiC and KfiD proteins. The subsequent transport of the polysaccharide onto the cell surface requires the KpsC, KpsD, KpsE, KpsM, KpsS and KpsT proteins, which are conserved between different group II capsular polysaccharides. The KfiA and KfiC, together with the KpsC, KpsS and KpsT proteins, were purified and polyclonal antisera to each protein generated. These antisera, together with one previously generated (by others) against the purified KfiD protein, were used in Western blot analysis to locate the corresponding proteins within the cell. Analysis of membrane fractions revealed that KfiA (involved in initiation of polysaccharide synthesis), Kf iC (K5 glycosyl transferase) and the Kf iD protein (UDP-glucose dehydrogenase) were associated with the inner membrane. The KpsC, KpsS and KpsT proteins involved in polysaccharide transport were associated with the inner membrane and this membrane association occurred in the absence of any other capsule-related proteins. The effect of mutations in individual kps genes on the localization of each protein was determined. Mutations in the kpC# kpsM, kpsS and kpsT genes resulted in a loss of membrane targeting for KfiA and KfiC, suggesting some form of hetero-oligomeric membrane-bound biosynthetic complex. Osmotic shock caused the release of KfiA, KfiC, KpsC and KpsS from the inner membrane into the periplasm, suggesting that the polysaccharide biosynthetic complex may be associated with sites of adhesion between the inner and outer membrane.
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- Pathogenicity And Medical Microbiology
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Resistance to cefotaxime and peptidoglycan composition in Enterococcus faecalis are influenced by exogenous sodium chloride
SUMMARY: The influence of NaCl on the susceptibility of Enterococcus faecalis to cefotaxime was tested with JH2-2, a laboratory strain, and 20 clinical strains grown on tryptic soy agar supplemented with 5% horse blood. Growth with 3% NaCl in the medium resulted in an increase in cefotaxime resistance and the appearance of a heterogeneous resistance phenotype: for the majority of the strains, the MlCs of cefotaxime increased from 4 to 512 pg m1-Y By a competition assay using cefotaxime and [3H]benzylpenicillin, it was shown for strain JH2-2 that at the MIC penicillin-binding protein (PBP) 2 and PBP3 were the apparent essential PBPs in medium without NaCI, whilst the low-affinity PBPs 4 and 1 were the apparent essential PBPs for cell growth in medium containing 3% NaCl. Analysis of JH2-2 peptidoglycan by HPLC and MS after growth in the presence of 3% NaCl showed a relative increase in unsubstituted monomers and a relative decrease in alanine- and dialanine-substituted monomers. It is therefore hypothesized that modification of the number of alanine-substituted precursors in the presence of NaCl could interfere with the functions of the different PBPs and thus play a role in cefotaxime resistance in E. faecalis.
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Antisense RNA to ahpC, an oxidative stress defence gene involved in isoniazid resistance, indicates that AhpC of Mycobacterium bovis has virulence properties
SUMMARY: Antisense RNA is a versatile tool for reducing gene expression. It was used to determine if ahpC, a gene that is involved in defence against oxidative stress and isoniazid (INH) resistance, is important for virulence of Mycobacterium bovis, a member of the Mycobecterium tuberculosis complex. Antisense RNA constructs of ahpC were made using different strength promoters in front of a reversed coding sequence of ahpC. These constructs were electroporated into a virulent wild-type M. bowis strain and a moderately virulent INH-resistant M. bo wis strain that was cata lase/peroxi dase-negat ive. Down- regulation of protein synthesis occurred and this was visualized by immunoblotting. All strains containing antisense RNA were markedly less virulent than their parent strains in guinea pigs. M. bowis with an up-regulated ahpC gene was more resistant to cumene hydroperoxide than its parent strain, which had a wild- type ahpC promoter. These results agree with a model of INH resistance in which overexpression of AhpC compensates in some INH-resistant strains for loss of catalase/peroxidase by maintaining the ability to defend against oxidative stress mediated through organic peroxides. In addition, normal expression of AhpC is crucial for maintaining the virulence of wild-type M. bovis, which has normal catalase/peroxidase levels.
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