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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The restriction map of Yersinia pestis pesticinogenicity plasmid pYP1 has been constructed with the use of 18 restriction endonucleases. Plasmid dimensions (6.3 Md) have been specified, the genes for pesticin synthesis, for pesticin immunity protein, fibrinolysin and plasmocoagulase have been localized by molecular cloning of single plasmid DNA fragments in vector plasmid pBR322.
Mol Gen Mikrobiol Virusol 1986 Apr
PMID:[Restriction map of pesticinogenicity plasmid pYP1 of Yersinia pestis]. 302 1

The techniques of electrophoresis in polyacrylamide gel and amino acid analysis permitted to find the slight difference in the composition of ribosomal proteins from Yersinia pestis and Escherichia coli cells. Ribosomal proteins were mapped and classified on the basis of two-dimensional electrophoresis data. Protein "X" was registered in the total ribosomal protein due to its separation in course of ribosomal subunits dissociation.
Mol Gen Mikrobiol Virusol 1988 Aug
PMID:[Comparative study of ribosomal proteins from Yersinia pestis and Escherichia coli: amino acid composition and electrophoretic mobility]. 305 58

The plasmids pCG86 and RP4elt coding for thermolabile enterotoxins of Escherichia coli (LT) were transferred in conjugation to Yersinia enterocolitica and Yersinia pseudotuberculosis cells. Both plasmids were stably inherited by the recipient cells. The elt genes of the toxins were expressed in Yersinia cells at the level comparable to the one registered in Escherichia coli cells. In the broth cultures of transconjugant cells the major part of LT toxin is bound with cells (74-97%). The obtained data may serve an experimental basis in favour of possibility of Ent+ strains of Yersinia enterocolitica and Yersinia pseudotuberculosis formation in nature and expediency of search and diagnosing of such strains.
Mol Gen Mikrobiol Virusol 1988 Aug
PMID:[Production of thermolabile enterotoxins of Escherichia coli by Yersinia enterocolitica and Yersinia pseudotuberculosis]. 305 60

The O-haptens of the major fraction (f5A) of B. abortus (Strains 2308 and 19) membrane bound smooth lipopolysaccharide (sLPS) were prepared by hydrolysis of f5A native sLPS in 1% acetic acid at 100 degrees C for 2 h. After hydrolysis, O-haptens were separated from Lipid A-protein complex by centrifugation, and from small fragments by ultrafiltration of molecular weight cut-off (MWCO) 1.0 X 10(3). These carbohydrate haptens were identified by precipitin-inhibition assay and further fractionated by both membrane filtration and dialysis. The size distributions of carbohydrate haptens of endotoxins (f5A) ranged from oligosaccharides up to polysacchandes of 1.0 X 10(4) MWCO. Three major fractions of MWCO 8.0-10.0 X 10(3), 3.5-5.0 X 10(3) and less than 1.0 X 10(3) from both strains 2308 and 19 contained more than 85% of the total immunoactive materials. These fractions of haptens were subjected to composition, proton and 13C NMR analysis and were found to be a homopolymer of alpha 1----2 linked, 4,5-dideoxy-4-formamido-D-mannose (N-formylperosamine), which is identical to O-haptens of B. abortus strain 119.3 and Yersinia enterocolitica serotype 0:9 and similar to Vibrio cholerae 569B (INABA). Fractions of these haptens exhibited similar inhibitory reactivities in a precipitin-inhibition assay as expressed as mumoles of monosaccharide of anhydro-N-formyl perosamine. They were about 480 times as active as Me alpha----DMan or DMan.
Mol Cell Biochem 1987 Jun
PMID:Structural and immunochemical characterization of the O-haptens of Brucella abortus lipopolysaccharides from strains 19 and 2308. 311 17

The efficiency of enumerating virulent Yersinia enterocolitica colonies was determined for 10 artificially contaminated foods by autoradiography after DNA colony hybridization using a 32P-labelled genetic probe and paper filters. Enumeration efficiency, which ranged from 0-98% (average 25 +/- 31% standard deviation), improved (42-138%, average 83 +/- 27% standard deviation) after enrichment with 0.5% KOH-0.5% NaCl. These efficiencies are equivalent to those obtained with nitrocellulose filters.
Mol Cell Probes 1988 Sep
PMID:Enumeration of virulent Yersinia enterocolitica colonies by DNA colony hybridization using alkaline treatment and paper filters. 322 83

Because bifunctional enzymes are distinctive and highly conserved products of relatively infrequent gene-fusion events, they are particularly useful markers to identify clusters of organisms at different hierarchical levels of a phylogenetic tree. Within the subdivision of gram-negative bacteria known as superfamily B, there are two distinctive types of tyrosine-pathway dehydrogenases: (1) a broad-specificity dehydrogenase (recently termed cyclohexadienyl dehydrogenase [CDH]) that can utilize either prephenate or L-arogenate as alternative substrates and (2) a bifunctional CDH that also posseses chorismate mutase activity. (T-proteins). The bifunctional T-protein, thought to be encoded by fused ancestral genes for chorismate mutase and CDH, was found to be present in enteric bacteria (Escherichia, Shigella, Salmonella, Citrobacter, Klebsiella, Erwinia, Serratia, Morganella, Cedecea, Kluyvera, Hafnia, Edwardsiella, Yersinia, and Proteus) and in Aeromonas and Alteromonas. Outside of the latter "enteric lineage," the T-protein is absent in other major superfamily-B genera, such as Pseudomonas (rRNA homology group I), Xanthomonas, Acinetobacter, and Oceanospirillum. Hence, the T-protein must have evolved after the divergence of the enteric and Oceanospirillum lineages. 3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase-phe, an early-pathway isozyme sensitive to feedback inhibition by L-phenylalanine, has been found in each member of the enteric lineage examined. The absence of both the T-protein and DAHP synthase-phe elsewhere in superfamily B indicates the emergence of these character states at approximately the same evolutionary time.
Mol Biol Evol 1988 May
PMID:The phylogenetic origin of the bifunctional tyrosine-pathway protein in the enteric lineage of bacteria. 338 29

Yersinia pestis plasmids having inserted Tn-movable elements and determining pesticinogenicity, Ca2+-dependence, production of mice toxin and fraction I have been mobilized for conjugal transfer into Y. pestis, Y. pseudotuberculosis or E. coli cells by plasmid pKA7. Plasmid determinants have been transferred with the frequencies 10-4-10-7 per donor cell. The plasmid DNA of high molecular mass has been identified in transconjugant cells. Plasmid mobilization in Yersinia pestis is supposed to be due to cointegrate formation of yersinia plasmids with R-plasmids.
Mol Gen Mikrobiol Virusol 1986 May
PMID:[Mobilization of plasmid determinants of Yersinia pestis using the plasmid pKA7]. 379 53

In recent years it has become clear that the production of N-acyl homoserine lactones (N-AHLs) is widespread in Gram-negative bacteria. These molecules act as diffusible chemical communication signals (bacterial pheromones) which regulate diverse physiological processes including bioluminescence, antibiotic production, plasmid conjugal transfer and synthesis of exoenzyme virulence factors in plant and animal pathogens. The paradigm for N-AHL production is in the bioluminescence (lux) phenotype of Photobacterium fischeri (formerly classified as Vibrio fischeri) where the signalling molecule N-(3-oxohexanoyl)-L-homoserine lactone (OHHL) is synthesized by the action of the LuxI protein. OHHL is thought to bind to the LuxR protein, allowing it to act as a positive transcriptional activator in an autoinduction process that physiologically couples cell density (and growth phase) to the expression of the bioluminescence genes. Based on the growing information on LuxI and LuxR homologues in other N-AHL-producing bacterial species such as Erwinia carotovora, Pseudomonas aeruginosa, Yersinia enterocolitica, Agrobacterium tumefaciens and Rhizobium leguminosarum, it seems that analogues of the P. fischeri lux autoinducer sensing system are widely distributed in bacteria. The general physiological function of these simple chemical signalling systems appears to be the modulation of discrete and diverse metabolic processes in concert with cell density. In an evolutionary sense, the elaboration and action of these bacterial pheromones can be viewed as an example of multicellularity in prokaryotic populations.
Mol Microbiol 1995 May
PMID:The bacterial 'enigma': cracking the code of cell-cell communication. 747 57

The virulence plasmid-encoded YopE cytotoxin of Yersinia pseudotuberculosis is secreted across the bacterial membranes and subsequently translocated into the eukaryotic cell. Translocation of YopE into target cells was recently shown to be polarized and only occurred at the zone of contact between the pathogen and the eukaryotic cell. Immunogold electron microscopy on cryosectioned Y. pseudotuberculosis revealed that YopE is secreted and deposited on the bacterial cell surface when the bacteria are grown in Ca(2+)-depleted media at 37 degrees C. No YopE was detected in the cytoplasm or in the membranes. In yerA mutants which are downregulated for YopE at a post-transcriptional level, the cytotoxin could only be detected in the cytoplasm. The overall recovery of YopE from the yerA mutant strain was, however, considerably lower than from the wild-type strain. yerA had no major effect on the translation of YopE, but was found to stabilize YopE in the cytoplasm. YerA was shown to specifically interact with YopE in the cytoplasm in vivo and this binding also correlated with YopE secretion. Targeting of YopE to the secretion loci as well as translocation of YopE into HeLa cells occurred also in the absence of YerA. Based on our findings, we suggest that YerA by binding to YopE stabilizes and maintains the cytotoxin in a secretion-competent conformation.
Mol Microbiol 1995 May
PMID:The chaperone-like protein YerA of Yersinia pseudotuberculosis stabilizes YopE in the cytoplasm but is dispensible for targeting to the secretion loci. 747 59

Previously, the PhoP-repressed locus prgH was identified as important for signalling epithelial cells to endocytose Salmonella typhimurium. Characterization of prgH revealed that it is an operon of four genes encoding polypeptides of 392 (prgH), 80 (prgI), 101 (prgJ) and 252 amino acid residues (prgK). Synthesis of the 2.6 kb prgHIJK transcript was repressed in bacteria that activate PhoP/PhoQ, indicating that PhoP/PhoQ regulates prgHIJK by transcriptional repression. The prgI, prgJ and prgK predicted gene products were similar to Shigella flexneri and Yersinia enterocolitica proteins required for secretion of Ipa and Yop virulence factors. Analysis of the culture supernatants from wild-type S. typhimurium demonstrated that at least 25 polypeptides larger than 14 kDa could be detected. In contrast, prgH1::TnphoA, phoP-constitutive and hil-deletion mutants had significant defects in their supernatant protein profiles. The invasion and supernatant protein profile defects of the prgH1::TnphoA mutant were both complemented by a 5.1 kb plasmid that included prgHIJK. These results suggest that PhoP/PhoQ regulates extracellular transport of proteins by transcriptional repression of secretion determinants and that secreted proteins may be involved in signalling epithelial cells to endocytose bacteria.
Mol Microbiol 1995 Jul
PMID:PhoP/PhoQ transcriptional repression of Salmonella typhimurium invasion genes: evidence for a role in protein secretion. 747 3


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