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PubMed2002

Structure of an extended-spectrum class A beta-lactamase from Proteus vulgaris K1.

The structure of a chromosomal extended-spectrum beta-lactamase (ESBL) having the ability to hydrolyze cephalosporins including cefuroxime and ceftazidime has been determined by X-ray crystallography to 1.75 A resolution. The species-specific class A beta-lactamase from Proteus vulgaris K1 was crystallized at pH 6.25 and its structure solved by molecular replacement. Refinement of the model resulted in crystallographic R and R(free) of 16.9 % and 19.3 %, respectively. The folding of the K1 enzyme is broadly similar to that of non-ESBL TEM-type beta-lactamases (2 A rmsd for C(alpha)) and differs by only 0.35 A for all atoms of six conserved residues in the catalytic site. Other residues promoting extended-spectrum activity in K1 include the side-chains of atypical residues Ser237 and Lys276. These side-chains are linked by two water molecules, one of which lies in the position normally filled by the guanidinium group of Arg244, present in most non-ESBL enzymes but absent from K1. The ammonium group of Lys276, ca 3.5 A from the virtual Arg244 guanidinium position, may interact with polar R2 substitutents on the dihydrothiazene ring of cephalosporins.

Binding Sites↗
PubMed1994

Cloning and expression in Escherichia coli of the gene encoding the Proteus vulgaris chondroitin ABC lyase.

The structural gene encoding chondroitin ABC lyase from Proteus vulgaris was cloned and sequenced. This gene consists of a single open reading frame of 3,063 bp, including a sequence (72 bp) for a possible secretory protein leader peptide, preceded by a Shine-Dalgarno ribosomal binding site. Promoter-like and rho-independent terminator sequences were detected upstream and downstream of the open reading frame, respectively. The G+C content of the coding region was 38.6%. The transcription startpoint was located 41-bp upstream of the initiation codon (ATG). Chondroitin ABC lyase is composed of 997 amino acids, and has a relative molecular mass of 112,635. When the 5.2-kb fragment containing the 1.2-kb upstream from the gene was inserted into pSTV29, and cloned in Escherichia coli, chondroitin ABC lyase was induced in the medium containing chondroitin-6-sulfate as the carbon source. On the other hand, when a 4.2-kb fragment containing only 0.2 kb upstream was inserted into pSTV29(pCHS delta 6), and pCHS delta 6 was introduced into E. coli, the enzyme was constitutively produced, even in medium containing glucose as the carbon source. By immunoblot analysis, the polypeptide synthesized by E. coli cells carrying pCHS delta 6 appeared to be the same as that of the purified chondroitin ABC lyase from P. vulgaris.

Amino Acid Sequence↗
PubMed1990

Nickel availability and urease expression in Proteus mirabilis.

Cells of Proteus mirabilis, previously grown in nutrient broth (NB), exhibited an increase in urease activity during subsequent incubation in mineral medium even when protein biosynthesis was inhibited. During growth in NB, degradation of amino acids obviously led to the formation of nickel-complexing metabolites, and nickel ions were therefore unavailable for maximal expression of enzymatically active urease; this inhibition of urease biosynthesis was overcome by the addition of nickel to the growth medium, and also by added glucose. Experiments concerning the incorporation of radioactive nickel into urease finally indicated that the observed increase in urease activity was caused by posttranslational insertion of nickel into performed apo-urease.

Amino Acids↗
PubMed1995

The specificity of the anti-Proteus antibody response in tissue-typed rheumatoid arthritis (RA) patients from Brest.

Anti-Proteus mirabilis antibody titres were found to be elevated in 50 active tissue-typed French rheumatoid arthritis (RA) patients from Brest when compared to 49 healthy French controls using enzyme-linked immunosorbent assay (ELISA; P < 0.001) and indirect immunofluorescence assay (IIFA; P < 0.001). However, there was no significant elevation in antibody titres against Escherichia coli or Salmonella typhimurium in the RA patients compared to the controls when measured by ELISA. Serum levels of C-reactive protein (CRP) were also found to be significantly higher in RA patients when compared to healthy control subjects (P < 0.001). These results suggest that P. mirabilis may play an important and specific role in the triggering and persistence of RA.

Adolescent↗
PubMed1976

Transcription of Escherichia coli ribosomal DNA in Proteus mirabilis.

Transcription of Escherichia coli ribosomal DNA introduced into Proteus mirabilis on F14 is described. We have developed an assay for E. coli coded ribosomal RNA involving fingerprinting of ribonuclease T1 digests of RNA isolated from ribosomal subunits. Sequence differences in the ribosomal RNA of the two species have allowed us to detect E. coli coded 16S, 23S, and 5S ribosomal RNA in ribosomal subunits of the E. coli-P. mirabilis hybrid. The proportion of E. coli coded rRNA in the hybrid is found at a level which is compatible with the number of E. coli (and P. mirabilis) ribosomal DNA sequences. The resulting ribosomal RNA appears in ribosomes in a form which indicates extensive compatibility of E. coli coded ribosomal RNA with P. mirabilis ribosomal proteins and maturational factors.

Base Sequence↗
PubMed1981

Repair and plasmid R46 mediated mutation requires inducible functions in Proteus mirabilis.

In Proteus mirabilis nalidixic acid or a predose of UV induce Rec protein formation, a portion of post-UV replication repair and "post-UV replication enhancement." These inducible functions are not significantly affected by the plasmid R46, which renders P. mirabilis efficiently UV-mutable. The R46-mediated UV induction of rif mutations requires additional inducible functions, as existing after nalidixic acid treatment in rec+ strains. After a nalidixic acid pretreatment UV efficient induction of rif mutations occurs without an otherwise obligatory period of post-UV incubation prior to plating on rifampicin agar. THe inducible character of this "qualification" of plasmid R46-mediated UV mutagenesis in P. mirabilis is evident from the inhibitory effects of chloramphenicol and starvation. Constitutive high-level synthesis of Rec protein in cells harboring the recombinant (multi-copy) rec+ plasmid pPM1 reduced plasmid R46-mediated UV mutagenesis, probably by preventing (inducible?) functions required by the plasmid R46 repair-mutator.

DNA Repair↗
PubMed1993

Proteus mirabilis biofilms and the encrustation of urethral catheters.

Bacterial biofilms were observed on 69 of 75 catheters taken from patients undergoing long-term bladder management. Ten catheters were colonized by pure cultures of Proteus mirabilis. In each of these cases the bacteria formed layers on the catheter surface, underlying encrustations of struvite and hydroxyapatite which partially or completely occluded the catheter lumen. Encrustation was also apparent on catheters colonized by P. mirabilis plus other species, but was rarely seen on catheters colonized by non-urease-producing species. These observations support the hypothesis that catheter encrustation is brought about by the activity of urease-producing biofilms and confirms that the main target in the control of catheter encrustation should be P. mirabilis.

Catheterization↗
PubMed1984

Anomalous expression of the E. coli lac operon in Proteus mirabilis. I. Effects of L8 and L8 UV5.

The lac operon shows anomalous expression in Proteus mirabilis: the maximal induced level is 10% or less of that in E. coli, while repression reduces this by a factor of only 2-5. We have sought to determine whether this effect relates in any way to CRP-mediated activation of expression, by comparing expression in P. mirabilis of lac operons (introduced for technical reasons on IncP1 plasmids) either regulatorily wild-type or bearing L8 or L8UV5. Derivatives of RP1 bearing L8UV5 were obtained by homogenotisation of pGC9114 (RP1::Tn951) in a L8UV5 background; while derivatives of RP4 bearing lac+, L8 or L8UV5 were obtained by Mu-mediated translocation of chromosomal regions bearing these alleles, following partial heat-induction of Mucts62 on pGM14 (RP4::Mucts62) in the appropriate hosts. These plasmids could be readily transferred to, and stably maintained in, the P. mirabilis strains employed. It was found that L8 reduced the maximal level of beta-galactosidase activity, and L8UV5 restored this activity to around wild-type, in P. mirabilis quantitatively very much as in E. coli. Nevertheless, the low maximal level of expression and high basal level characteristic of the former host were unchanged. The simplest explanation of these results is that P. mirabilis contains a protein that mimics the E. coli CRP protein in interacting with the appropriate DNA binding site and thereby stimulating transcription; and that the anomalous regulation of lac in this host is unconnected with the CRP system.

Escherichia coli↗
PubMed1984

Anomalous expression of the E. coli lac operon in Proteus mirabilis. II. Effects of lacI and lacP mutations.

The lac operon introduced into Proteus mirabilis shows two anomalies of expression: the maximal induced level is reduced by about an order of magnitude, and the basal level becomes about 100 times higher than in E. coli, as a result of which the induction ratio appears very small, around 2-5 in contrast to as much as 1000 in E. coli. It was suggested by Baumberg and Dennison (1975) that the two anomalies might be manifestations of a single effect whereby some exogenous promoters give poor expression in this host, since they could result from poor expression of the lacZYA and lacI promoters respectively. We show here that when the lacP class II promoter mutation L305 was transferred on an F-prime into P. mirabilis, its effect on lac expression was much as in E. coli. However, when Flac bearing the IQ1 up-promoter mutation was introduced into P. mirabilis, the basal level decreased by three orders of magnitude, in accord with poor expression of lacI+ being responsible for the usual low induction ratio. These results are consistent with the hypothesis of Baumberg and Dennison (1975) but do not prove it: poor expression of lacI and/or lacZYA could also result from weak translation initiation, problems of continuation of transcription or translation (e.g. due to pause sequences or differences in codon use), or diminished mRNA stability.

Escherichia coli↗
PubMed1988

Identification of the promoters directing in vivo expression of hemolysin genes in Proteus vulgaris and Escherichia coli.

The hemolytic activity of Escherichia coli and Proteus vulgaris is determined by common contiguous genes encoding synthesis (hly C, hly A) and specific secretion (hly B, hly D) of active hemolysin. Nevertheless, the hly C-proximal DNA sequences directing production of the homologous hemolysins by the recombinant DNAs P. vulgaris pVU763-709 and E. coli pANN202-312 showed no extensive homology. Primer extension and S1 nuclease protection were used to define in the two sequences the 5' termini of hly transcripts synthesized in vivo and thus to infer the active hly promoters sequences. The E. coli hly C upstream region contained three separate promotors directing in vivo hly transcription, while the corresponding transcription of the P. vulgaris hly operon originated from a single distinct promotor, the -35 and -10 sequences of which formed part of an inverted repeat sequence. Elevated hemolytic activity caused by upstream Tn5 insertions in pVU763-709 resulted from increased transcription from this promotor.

Base Sequence↗
PubMed1982

Interspecies recA protein substitution in Escherichia coli and Proteus mirabilis.

With the help of recombinant plasmids carrying the recA gene of Escherichia coli or of Proteus mirabilis the ability of the recA gene products to substitute functionally for each other was studied. The recA protein of each can function in recombination, repair, induction of mutations and prophages and in regulation of its own synthesis within the foreign host nearly equally well as in the natural host. It is, therefore, suggested that recA-dependent processes act similarly in E. coli and P. mirabilis.

Bacterial Proteins↗
PubMed1987

Cloning and DNA sequence determination of the L11 ribosomal protein operon of Serratia marcescens and Proteus vulgaris: translational feedback regulation of the Escherichia coli L11 operon by heterologous L1 proteins.

In Escherichia coli the genes encoding ribosomal proteins L11 (rplK) and L1 (rplA) are contained in a single operon and their expression is translationally regulated by L1. We have cloned the homologous genes from two other enterobacteria, Serratia marcescens and Proteus vulgaris, and determined nucleotide sequences. The genes are organized in a similar way to that found in E. coli. Conservation of nucleotide and amino acid sequences relative to E. coli in the protein coding regions are 89.2% and 94.7% for S. marcescens, and 80.9% and 88.6% for P. vulgaris. Nucleotide sequences of L11 mRNA leader regions were strongly conserved for the primary as well as the secondary structures in the L1 target site. We have also constructed plasmids carrying E. coli L11 and either P. vulgaris or S. marcescens L1 genes fused to the lac promoter, with or without the E. coli leader containing the L1 target site. Induction of transcription of the operons possessing the E. coli mRNA leader did not lead to overproduction of L11, indicating translational regulation of the chimeric operon as well as the chromosomal operon by the plasmid encoded L1. Repression of the chromosomal L11 operon was directly demonstrated upon induction of the chimeric operons without the leader, which also lack the L11 initiation signal but have a mutation allowing L1 translation.(ABSTRACT TRUNCATED AT 250 WORDS)

Base Sequence↗
PubMed1988

Comparison of the haemolysin secretion protein HlyB from Proteus vulgaris and Escherichia coli; site-directed mutagenesis causing impairment of export function.

The hlyB secretion genes of Proteus vulgaris and Escherichia coli showed 81% nucleotide homology and similar E. coli-atypical codon usage. The deduced protein sequences differed in 54 of 707 residues and shared a previously unreported sequence which corresponds to the ATP-binding motif characteristic of protein kinases. The motif was also conserved in the HlyB of Morganella morganii. Of 4 oligonucleotide-directed substitutions introduced into the putative E. coli HlyB motif, 2 non-conservative changes caused radical reductions in the export of active haemolysin protein.

Amino Acid Sequence↗
PubMed1984

Functional substitution of the recE gene of Bacillus subtilis by the recA gene of Proteus mirabilis.

Rec mutants of Bacillus subtilis have been tested for complementation by the recA gene of Proteus mirabilis (recApm) which was introduced into B. subtilis via the plasmid pHP334. In the recE4 mutant of B. subtilis the plasmid pHP334 restored significantly the defects in RecE functions tested: UV-sensitivity, homologous recombination (transduction and transformation) and prophage induction. Although serological methods to detect the presence of RecApm protein in B. subtilis have been unsuccessful, our results strongly indicate that the recE function of B. subtilis is analogous to the recA function of P. mirabilis.

Bacillus subtilis↗
PubMed1994

Application of 1D and 2D NMR techniques to the structure elucidation of the O-polysaccharide from Proteus mirabilis O:57.

The LPS O-polysaccharide (O-PS) produced by Proteus mirabilis serotype O:57 (ATCC 49995) was shown by NMR spectroscopy and chemical analysis to be a high-molecular-weight acidic branched polymer of pentasaccharide repeating units, composed of D-glucose, D-galactose, 2-acetamido-2-deoxy-D-galactose and glycerophosphate residues (1:2:2:2:1). Application of one- and two-dimensional NMR methods allowed the complete assignment of notoriously crowded 1H and 13C spectra of the O-PS, leading to the determination of its structure. Several of the NMR techniques used were applied for the first time to the structure elucidation of polysaccharides. The resonances of galactose H5, H6 and H6' were identified by a 1D analog of 3D NOESY-TOCSY and 2D (1H,1H) triple-quantum experiments. The position and the nature of the phosphate group were determined from 2D 31P (omega 1)-half-filtered COSY and 2D 31P-relayed COSY spectra. 2D HMQC-TOCSY and 2D single-quantum proton-carbon long-range correlation techniques were used to overcome the difficulties of severe overlap and higher order effects in the 1H NMR spectrum of the O-PS. The latter technique, together with 2D NOESY, enabled us to identify the substitution positions, the anomeric configurations and the sequence of the component glycose residues in the O-PS.

Carbohydrate Conformation↗
PubMed1983

Electron transport and cytochromes in aerobically grown Proteus mirabilis.

The function of the cytochromes in electron transport from NADH to oxygen in aerobically grown Proteus mirabilis has been determined. 77K-Spectra of cytoplasmic membrane suspensions, frozen while catalyzing electron transport from NADH to oxygen, in the presence as well as in the absence of 2-n-heptyl-4-hydroxyquinoline-N-oxide, have been recorded. Analysis of these 77K-spectra revealed that cytochrome b-563 (E'0 = +140 mV), cytochrome b-556 (E'0 = +140 mV) [or alternatively cytochrome b-563/556 (E'0 = +140 mV)] and cytochrome b-557 (E'0 = +50 mV) may function in a Q or b-cycle. The function of cytochrome c-549 (E'0 = +75 mV), which seems to be present only in a very low concentration, and cytochrome b-556 (E'0 = -105 mV), which reacts very slowly to the addition of NADH and oxygen, remains unclear. Cytochrome o, the main oxidase of aerobically grown P. mirabilis cells, can not be detected by the methods described above. Only when the reduced form of cytochrome o is liganded with carbon monoxide a specific alpha-band can be detected at 569 nm at 25 degrees C and 565 nm at 77K.

Cytochrome b Group↗
PubMed1984

In vitro synthesis of peptidoglycan by spheroplasts of Proteus mirabilis grown in the presence of penicillin.

Spheroplasts of the unstable L-form of Proteus mirabilis with fragile, shape defective cell walls grown in medium containing 120 mg/l penicillin G and then killed and permeabilized by ether treatment, were capable of in vitro synthesis of peptidoglycan from the precursors UDP-GlcNAc and UDP-MurNAc-L-Ala-D-Glu(ms-A2pm-D-Ala-D-Ala). The in vitro peptidoglycan was extensively peptide-crosslinked, indicating a continuing function of peptidoglycan transpeptidase in the spheroplasts. The seven penicillin-binding proteins (PBPs) of P. mirabilis with their functions as multiple peptidoglycan transpeptidases were shown to be saturated in the spheroplasts and thereby functionally inactivated by the penicillin of the growth medium to a very different degree. Complete or almost complete saturation occurred with the PBPs 1A, 1B, and 3, for which functions as indispensable transpeptidases in Escherichia coli have been postulated. In contrast, PBPs 5 and 6 were not saturated in the L-form spheroplasts. Transpeptidase function has been described previously in PBP 5 of P. mirabilis. The working hypothesis is proposed that synthesis of the functionally defective peptidoglycan of L-form spheroplasts in the presence of penicillin takes place with transpeptidase function of PBP 5.

Acetylation↗
PubMed1984

Dimethylsulphoxide and trimethylamine oxide respiration of Proteus vulgaris. Evidence for a common terminal reductase system.

Dimethylsulphoxide (DMSO) and trimethylamine oxide (TMAO) sustained anaerobic growth of Proteus vulgaris with the non-fermentable substrate lactate. Cytoplasmic membrane vesicles energized by electron transfer from formate to DMSO displayed anaerobic uptake of serine, which was hindered by metabolic inhibitors known to destroy the proton motive force. This showed that DMSO reduction was coupled with a chemiosmotic mechanism of energy conversion; similar data for TMAO respiration have been presented previously. All biochemical tests applied indicated that the oxides were reduced by the same reductase system. The DMSO and TMAO reductase activities showed the same mobility on ion-exchange chromatography, and polyacrylamide disc gel electrophoresis (pH 8.9), gradient gel electrophoresis, and gel isoelectric focusing; mol. wt. and pI determined were 95,000 and 4.6, respectively. DMSO inhibited reduction of [14C]TMAO in vesicles. The reductase was inducible to a certain extent; both oxides being equally efficient as inducers. TMAO was reduced at a higher rate than DMSO, explaining faster growth of cells and increased uptake of serine in vesicles with TMAO as electron acceptor. Comparative studies with Escherichia coli also gave evidence for common TMAO and DMSO reductase systems.

Anaerobiosis↗