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PubMed1989

N-terminal region of Proteus mirabilis glutathione transferase is not homologous to mammalian and plant glutathione transferases.

The N-terminal amino acid sequence of glutathione transferase, Pm-GST-6.0, purified from Proteus mirabilis [(1988) Biochem. J. 255, 971-975] up to residue 38 and a comparative peptide fingerprint are reported. No obvious homology with the sequences of alpha, pi and mu classes of mammalian glutathione transferases as well as with those of plant glutathione transferases has been noted. These results suggest that the classification so far adopted for glutathione transferases cannot be extended to the bacterial enzyme.

Amino Acid Sequence↗

PubMed1994

Immunogold localization of glutathione transferase B1-1 in Proteus mirabilis.

By using the immunolabelling technique, the cellular localization of glutathione transferase in Proteus mirabilis was investigated. Evidence was obtained indicating a significant higher content of glutathione transferase in the periplasmic than cytoplasmic space. This result further support the idea that bacterial glutathione transferase is involved in xenobiotic detoxication.

Blotting, Western↗

PubMed1996

Structures of new acidic O-specific polysaccharides of the bacterium Proteus mirabilis serogroups O26 and O30.

The polysaccharide chains of the lipopolysaccharides of the Proteus mirabilis serogroups O26 and O30 were studied using sugar and methylation analysis and 1H and 13C NMR spectroscopy, including two-dimensional correlation spectroscopy and rotating-frame NOE spectroscopy. The polysaccharides were found to be acidic due to the presence of D-galacturonic acid and its amide with L-lysine in serogroup O26 or D-glucuronic acid in serogroup O30, and the structures of their tetrasaccharide repeating units were established. The O26-specific polysaccharide is structurally and serologically related to the O-specific polysaccharide of P. mirabilis O28, which includes amides of D-GalA with L-lysine and L-serine [Radziejewska-Lebrecht, J. et al. (1995) Eur. J. Biochem. 230, 705-712].

Carbohydrate Conformation↗

PubMed1985

Evolution of the lipoprotein gene in the enterobacteriaceae. Cloning and DNA sequence of the lpp gene from Proteus mirabilis.

We cloned the lipoprotein gene from Proteus mirabilis and determined its DNA sequence. Comparison with the lpp genes from Escherichia coli, Serratia marcescens, Erwinia amylovora and Morganella morganii revealed several unique features of the evolution of the lpp gene in the Enterobacteriaceae and enabled us to establish phylogenetic relationships between these bacteria.

Base Composition↗

PubMed1986

Crystallization of recA protein from Proteus mirabilis.

The recA protein from Proteus mirabilis, which is homologous to the Escherichia coli protein, forms crystals in the orthorhombic space group P2(1)2(1)2(1). There are two 38,000 molecular weight subunits in the asymmetric unit and the unit cell dimensions are a = 57.5, b = 127.0 and c = 157.0 A.

Crystallography↗

PubMed1991

Crystallization and crystal packing of Proteus mirabilis PR catalase.

The tetrameric catalase from Proteus mirabilis PR (EC 1.11.1.6), known to bind NADPH, has been crystallized by the hanging-drop method in a form apparently depleted in dinucleotide. The crystals belong to the hexagonal space group P6(2)22 with a = b = 111.7 A, c = 248.8 A. There is one subunit in the asymmetric unit. Data were collected to 2.9 A at the L.U.R.E. (Orsay) synchrotron radiation facility. The tetramers have been located in the crystal, centered on the site (1/2, 0, 0) with 222 symmetry.

Catalase↗

PubMed1987

Reactions of hemocytes of immune and non-immune Galleria mellonella larvae to Proteus mirabilis.

Immune larval Galleria mellonella removed live Proteus mirabilis from the hemolymph less effectively than did non-immune larvae. This was attributed to a decline in total hemocyte counts, levels of plasmatocytes and granulocytes and hemocyte adhesion capacity. Immune serum possessed factors which reduced bacterial adhesion to the hemocytes. This was not due to altering bacterial surfaces but rather to irreversible suppression of hemocyte activity.

Animals↗

PubMed1987

Cloning and expression of the gene(s) for chromosome-mediated beta-lactamase production of Proteus vulgaris in Escherichia coli.

The gene(s) for chromosome-mediated beta-lactamase production of Proteus vulgaris GN7919 was cloned into a unique EcoRI site of pACYC184 as an insert of a 14.2-kb fragment, which was further digested into two fragments with EcoRI, 4.9 and 9.3 kb. The restriction enzyme digestion pattern of the recombinant plasmid, designated pMS182, had no similarity to those of other chromosomal beta-lactamase genes cloned from gram-negative bacteria. Plasmid pMS182 enabled host Escherichia coli ML4953 to inducibly produce beta-lactamase which was identical to that of the parent P. vulgaris in substrate profile, molecular weight, and reactivity to antiserum raised against P. vulgaris GN7919 beta-lactamase. The pMS182-harboring E. coli were highly resistant to beta-lactam antibiotics, possibly based on inducible production of beta-lactamase.

Chromosomes, Bacterial↗

PubMed1995

Simulations of electron transfer in the NADPH-bound catalase from Proteus mirabilis PR.

Catalase-bound NADPH both prevents and reverses the accumulation of compound II, an inactive form of catalase that is generated from the normal active intermediate form (compound I) when catalase is exposed to a steady flow of hydrogen peroxide. The mechanism for the regeneration reaction is unknown although NADPH could act either as a one-electron or a two-electron donor. Recently, a reaction scheme has been proposed in which the formation of compound II from compound I generates a neighboring radical species within the protein. NADPH would then donate two electrons, one to compound II for reduction of the iron and the other to the protein free radical. In this paper, we report calculations to find the dominant electron tunneling pathways between NADPH and the heme iron in the catalase from the peroxide-resistant mutant of Proteus mirabilis. Two major tunneling pathways are found which fuse together on Ser-196. It is suggested that the sequence Gly-Ser of the loop that divides the beta 5-strand is the key element for shielding a radical amino acid.

Algorithms↗

PubMed1991

The recA-recBCD dependent recombination pathways of Serratia marcescens and Proteus mirabilis in Escherichia coli: functions of hybrid enzymes and hybrid pathways.

The physical maps of cloned recBCD gene regions of Serratia marcescens and Proteus mirabilis were correlated to genes located in this region. The genes thyA, recC, recB, recD and argA were organized as in Escherichia coli. The 3 rec genes code for the 3 different subunits of the RecBCD enzyme and produced enzymes promoting recombination and repair of UV damage in E coli. The recBCD-dependent stimulation of recombination at specific nucleotide sequences called Chi (Chi-activation) was determined in lambda red-gam-crosses. Chi-activation by the different RecBCD enzymes decreased in the order E coli greater than S marcescens greater than P mirabilis. In E coli cloned subunits genes from S marcescens and P mirabilis led to the formation of functional hybrid enzymes consisting of subunits from 2 or even 3 species. The origin of the RecC subunit present in the hybrid enzymes affected the degree of Chi-activation. Further, changes in Chi-activation occurred when the RecD subunit in the enzyme from E coli was replaced by RecD proteins from S marcescens or P mirabilis. This suggested that the RecD subunit determines not only whether or not Chi-activation is possible but also to which extent it occurs. Finally we have reconstituted recombination pathways of S marcescens and P mirabilis by combining the cloned recA and recBCD genes from these species in E coli deleted for recA and recBCD. Both pathways can efficiently promote recombination and repair. Studies are summarized which showed that levels of repair and recombination promoted by the recA-recBCD genes are mostly higher when the recA and recBCD genes came from the same species than from 2 different species (hybrid RecBCD recombination pathway). The data are interpreted to provide evidence that in vivo the RecA protein co-operates with the RecBCD enzyme in recombination and repair of UV damage.

Chromosome Mapping↗

PubMed1979

Alterations in the cell envelope composition of Proteus mirabilis during the development of swarmer cells.

Long, swarming cells of Proteus mirabilis had different proportions of some lipopolysaccharide components when compared to short cells, either agar grown or broth grown. Fluorescence spectrophotometry of antibody binding, and sodium dodecyl sulphate-polyacrylamide gel electrophoresis indicated that the change was in the proportion of lipopolysaccharide with long O-antigenic sidechains, swarmer lipopolysaccharide relative to short sidechain lipopolysaccharide than the non-swarming cells. The proteins and phospholipids of the envelop remained the same during swarmer development. The results are discussed in relation to the increase in flagella synthesis and permeability to some antibacterial agents during swarmer development.

Binding Sites, Antibody↗

PubMed1989

Heterologous signal peptide processing in fusion interferon synthesis by engineered L-forms of Proteus mirabilis.

A recombinant DNA Proteus mirabilis L-form expression system, LVI (pJS127), was used to synthesize human fusion interferon alpha 1 (f-IFN-alpha 1). In the expression plasmid used, the complete coding sequence of IFN-alpha 1 was linked to the streptococcal speA promoter and the 5' end of the speA structural gene including its signal sequence coding region. LVI (pJS127) was capable of complete secretion into the culture medium of biologically active f-IFN-alpha 1 whose identity was confirmed by immunological and chemical evidence. In particular, bacterial L-forms were for the first time shown to be capable of correct signal peptide processing, as determined by N-terminal sequencing of the secreted f-IFN.

Amino Acids↗

PubMed1990

Cloning of the genes encoding urease from Proteus vulgaris and sequencing of the structural genes.

A fragment of chromosomal DNA from proteus vulgaris encoding urease was cloned and expressed in Escherichia coli. A 3 kbp region was sequenced and revealed three open reading frames with homology to jack bean (Canavalia ensiformis) urease. The smallest protein (11 kDa) was homologous to the N-terminus of the plant enzyme and the largest polypeptide (61 kDa) corresponded to the C-terminus. The large protein contained conserved regions and a cysteine residue which is known to be catalytically important in the plant enzyme. A protein of 12 kDa showed homology to residues 132 to 237 of jack bean urease.

Amino Acid Sequence↗

PubMed1995

Heavy metal effects on Proteus mirabilis superoxide dismutase production.

Proteus mirabilis expressed three superoxide dismutase activities, which depended on the level of soluble iron and dioxygen in the culture medium. Cadmium and lead decreased production of super oxide dismutase in liquid culture and on solid medium. A fourth super oxide dismutase activity appeared in extracts from cells grown in the presence of cadmium. These results support the idea of an interaction between toxic metal ions and putative iron- and redox-dependent regulatory systems.

Cadmium↗

PubMed1981

Cloning of a recA-like gene of Proteus mirabilis.

A gene of Proteus mirabilis that can substitute for functions of the recA gene of Escherichia coli has been cloned into the plasmid pBR322, using shotgun experiments. The recA-like gene (recAp.m.) has been localized by restriction mapping within a 1.5-Md PstI fragment that is a part of two cloned HindIII fragments of the chromosome of P. mirabilis. The restriction map of the recAp.m. gene differs from that of the recA gene of E. coli. Functionally, the recombinant plasmids containing the recAp.m. gene restore a nearly wild-type level of UV-resistance to several point and deletion mutants in the recA gene of E. coli.

Chromosome Mapping↗

PubMedDate not supplied

Molecular cloning of Proteus morganii phenylalanine deaminase gene in Escherichia coli.

The gene for phenylalanine deaminase (PAD) of Proteus morganii strain 2815 has been isolated on a 6.3-kb HindIII restriction fragment and cloned within RP4-prime plasmids, pYB2321 and pYB2322, in both orientations. Expression of the cloned gene in Escherichia coli strains was comparable to that in P. morganii 2815. The hybrid plasmids mobilized the 2815 chromosome with trajectories in reverse directions from an origin between ser-2 and ade-1, suggesting the map location of the PAD gene.

Amino Acid Oxidoreductases↗

PubMed1987

IS431, a staphylococcal insertion sequence-like element related to IS26 from Proteus vulgaris.

We present the nucleotide sequence of IS431, a new staphylococcal insertion sequence-like element flanking the mercury-resistance determinant of pI524 and associated with the methicillin-resistance determinant. IS431 left is 800 bp long and has a perfect terminal inverted repeat (IR) of 22 bp; IS431 right is 786 bp long and has a terminal IR homologous to the IR of IS431 left except that the terminal 8 bp are absent. Both IRs share a 10-bp homology with the IR of IS26 from Proteus vulgaris. No directly repeated sequences were detected immediately adjacent to the IRs. An open reading frame (ORF) of 675 bp spans most of the IS431 sequence. Its deduced amino acid (aa) sequence shows 40% homology to the 234-aa-long putative transposase coded by ORFI of IS26.

Animals↗

PubMed1990

Nucleotide sequence of a Proteus mirabilis DNA fragment homologous to the 60K-rnpA-rpmH-dnaA-dnaN-recF-gyrB region of Escherichia coli.

A 6.5-kb DNA fragment from Proteus mirabilis hybridized to the Escherichia coli dnaA gene. This DNA fragment was cloned and the nucleotide (nt) sequence determined. The fragment is homologous to a region of the E. coli chromosome containing a part of the gene encoding a 60-kDa membrane-associated protein (60K), the rnpA-rpmH-dnaA-dnaN-recF genes, and the N-terminal part of the gyrB gene. The degree of homology is variable: the amino-acid (aa) sequence of a part of the 60K protein and a part of the DnaA protein is only minimally conserved, whereas the C-terminal 148 aa of DnaA are identical in the two species. The conservation of the nt sequence between the rnpA gene and the gene encoding the 60K protein suggests that this region encodes a hitherto unrecognized protein. The ORF for this protein partially overlaps the 3' end of the rnpA structural gene, and the degree of conservation suggests that this gene is important for these bacteria.

Amino Acid Sequence↗