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J Bardowski

Publications and source records attributed to J Bardowski.

12 recordsLinked to original sources
PubMed2007

Mosaic structure of p1658/97, a 125-kilobase plasmid harboring an active amplicon with the extended-spectrum beta-lactamase gene blaSHV-5.

Escherichia coli isolates recovered from patients during a clonal outbreak in a Warsaw, Poland, hospital in 1997 produced different levels of an extended-spectrum beta-lactamase (ESBL) of the SHV type. The beta-lactamase hyperproduction correlated with the multiplication of ESBL gene copies within a plasmid. Here, we present the complete nucleotide sequence of plasmid p1658/97 carried by the isolates recovered during the outbreak. The plasmid is 125,491 bp and shows a mosaic structure in which all modules constituting the plasmid core are homologous to those found in plasmids F and R100 and are separated by segments of homology to other known regions (plasmid R64, Providencia rettgeri genomic island R391, Vibrio cholerae STX transposon, Klebsiella pneumoniae or E. coli chromosomes). Plasmid p1658/97 bears two replication systems, IncFII and IncFIB; we demonstrated that both are active in E. coli. The presence of an active partition system (sopABC locus) and two postsegregational killing systems (pemIK and hok/sok) indicates that the plasmid should be stably maintained in E. coli populations. The conjugative transfer is ensured by the operons of the tra and trb genes. We also demonstrate that the plasmidic segment undergoing amplification contains the blaSHV-5 gene and is homologous to a 7.9-kb fragment of the K. pneumoniae chromosome. The amplicon displays the structure of a composite transposon of type I.

DNA, Bacterial↗
PubMed1998

Multiple transcriptional control of the Lactococcus lactis trp operon.

The Lactococcus lactis trpEGDCFBA operon is preceded by a noncoding leader region. Transcriptional studies of the trp operon revealed three transcripts with respective sizes of 8 kb (encompassing the entire operon), 290 bases, and 160 bases (corresponding to parts of the leader region). These transcripts most likely result from initiation at the unique Ptrp promoter, transcription termination at either T1 (upstream of the trp operon) or T2 (downstream of the trp operon), and/or processing. Three parameters were shown to differentially affect the amount of these transcripts: (i) following tryptophan depletion, the amount of the 8-kb transcript increases 300- to 500-fold; (ii) depletion in any amino acid increased transcription initiation about fourfold; and (iii) upon entry into stationary phase the amount of the 8-kb transcript decreases abruptly. The tryptophan-dependent transcription control is exerted through transcription antitermination.

Base Sequence↗
PubMed1994

BglR protein, which belongs to the BglG family of transcriptional antiterminators, is involved in beta-glucoside utilization in Lactococcus lactis.

A fragment of the Lactococcus lactis chromosome containing an open reading frame of 265 codons, denoted bglR, has been characterized. The polypeptide encoded by bglR shares 36 to 30% sequence identity with a family of regulatory proteins including ArbG from Erwinia chrysanthemi, BglG from Escherichia coli, and SacT and SacY from Bacillus subtilis. These regulatory proteins are involved in positive control of the utilization of different sugars by transcription antitermination. For some of these regulatory proteins it has been demonstrated that antitermination is exerted by binding to a conserved RNA sequence, partially overlapping the transcription terminator and thus preventing transcription termination. Upstream of bglR, we identified a transcription terminator whose 5' end was overlapped by a 32-bp sequence, highly homologous to the RNA-binding site that is conserved in other regulatory systems. Constitutive expression of bglR in E. coli increased the expression of a bglG::lacZ transcriptional fusion. The fact that that the expression of BglG is autoregulated in E. coli suggests that BglG and BglR are functionally equivalent. In L. lactis, we observed that (i) the expression of a bglR::lacZ fusion is increased by beta-glucoside sugars, (ii) disruption of bglR impairs growth on some beta-glucosides, and (iii) the expression of bglR is positively autoregulated. Because of these structural and functional similarities between BglR and the transcription antiterminators of the BglG family, we propose that BglR may be the lactococcal counterpart of the E. coli BglG regulator of beta-glucoside utilization.

Amino Acid Sequence↗
PubMed1993

Gene inactivation in Lactococcus lactis: branched-chain amino acid biosynthesis.

The Lactococcus lactis subsp. lactis strains isolated from dairy products are auxotrophs for branched-chain amino acids (leucine, isoleucine, and valine), while most strains isolated from nondairy media are prototrophs. We have cloned and sequenced the leu genes from one auxotroph, IL1403. The sequence is 99% homologous to that of the prototroph NCDO2118, which was determined previously. Two nonsense mutations and two small deletions were found in the auxotroph sequence, which might explain the branched-chain amino acid auxotrophy. Nevertheless, the leu genes from the auxotroph appear to be transcribed and regulated similarly to those from the prototroph.

Amino Acid Sequence↗
PubMed1992

Tryptophan biosynthesis genes in Lactococcus lactis subsp. lactis.

The Lactococcus lactis chromosomal region containing the seven structural genes required for tryptophan biosynthesis was characterized by cloning and sequencing. All of the trp genes were identified by the homology of their products with known Trp proteins from other organisms. The identification was confirmed for five genes by their ability to complement trp mutations in Escherichia coli. The seven structural genes are present in the order trpEGDCFBA and span a 7,968-bp segment. Each gene is preceded by a putative ribosome binding site complementary to the 3' end of the L. lactis 16S rRNA. Three pairs of genes (trpG-trpD, trpC-trpF, and trpB-trpA) overlap, and there is intercistronic spacing of 124, 46, and 585 bp between the trpE-trpG, trpD-trpC, and trpF-trpB gene pairs, respectively. No gene fusion was found. Upstream of the trp genes, a 457-bp noncoding DNA segment contains several regions fitting the consensus for gram-positive promoters and one region strongly resembling a transcription terminator. However, it seems unlikely that an attenuation mechanism similar to the one found in E. coli regulates tryptophan biosynthesis in L. lactis, since no potential leader peptide was detected. We propose that a mechanisms resembling that described in Bacillus spp. can regulate trp genes expression in L. lactis.

Amino Acid Sequence↗
PubMed1985

Chromosomal localization of resistance to fosfomycin and aminocyclitol antibiotics in hospital strains of Staphylococcus aureus.

The chromosomal localization of fosfomycin resistance genes in three hospital Staphylococcus aureus strains and in the standard strain NCTC 8507 was shown. Moreover, the chromosomal locus of the gene determining resistance to three aminocyclitol antibiotics: gentamycin, kanamycin and tobramycin in the one of hospital strains was determined. The possibility of transducing this resistance and the absence of plasmid DNA in the obtained transductants, suggest transposomal nature of the gene determining gentamycin, kanamycin and tobramycin resistance in the investigated strain.

Anti-Bacterial Agents↗
PubMed1981

Preliminary attempts at bacteriocin typing of lactic streptococci.

Preliminary attempts at typing Streptococcus lactis, S. lactis subsp. diacetylactis and Streptococcus cremoris strains by bacteriocins (lactostrepcins) are presented. Among 106 strains used about 85% were sensitive to lactostreptocins. The highest proportion of bacteriocin-typing strains was observed in S. lactis species. Lactostrepcin-sensitive strains could be divided into 6 types. The results confirm some individual features of S. diacetylactis compared with S. lactis.

Bacteriocins↗
PubMed1978

Lactostrepcins--acid bacteriocins produced by lactic streptococci.

All 47 non-nisin producing strains of Streptococcus lactis and 12/13 strains of Str. lactis subsp. diacetylactis examined produced bacteriocins, for which the term lactostrepcins is suggested. Seven strains of Str. cremoris examined produced no bacteriocins active against 3 lactic streptococci strains used as indicators. The strains examined were divided into 3 groups: I, those producing lactostrepcins active against only one streptomycin resistant mutant of Str. lactis 60 indicator strain; II, those producing lactostrepcins active against all 3 indicator strains; III, those not producing lactostrepcins active against the indicator strains employed. The lactostrepcins were sensitive to various proteolytic enzymes and to phospholipase D, but retained full or partial activity after dialysis. Most of the bacteriocins studied were fully active only within the pH range 4.2--5.0 and were reversibly inactivated at pH 7.0 or 8.0. Results suggested occurrence of 4 different lactostrepcins. The lactostrepcins produced by all group I strains were the same, but there were differences among the lactostrepcins produced by group II strains. Lactostrepcins killed some beta-haemolytic streptococci and some strains of Lactobacillus helveticus. One of the lactostrepcins was also active against certain Leuconostoc strains, but not against other Leuconostoc strains, nor against L. helveticus or other Gram-positive bacteria.

Bacteriocins↗