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  • Articles  (9,721)
  • Springer Nature  (9,484)
  • Blackwell Publishing Ltd  (237)
  • American Institute of Physics
  • 1995-1999  (5,863)
  • 1980-1984
  • 1970-1974  (3,858)
  • 1960-1964
  • 1998  (5,863)
  • 1971  (3,858)
  • Medicine  (9,721)
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  • Articles  (9,721)
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  • 1995-1999  (5,863)
  • 1980-1984
  • 1970-1974  (3,858)
  • 1960-1964
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  • 1
    Electronic Resource
    Electronic Resource
    Nucleoside diphosphate kinase: role in bacterial growth, virulence, cell signalling and polysaccharide synthesis (1998)
    Oxford BSL : Blackwell Publishing Ltd
    Molecular microbiology 28 (1998), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Nucleoside diphosphate kinase (Ndk) is an important enzyme that generates nucleoside triphosphates (NTPs) or their deoxy derivatives by terminal phosphotransfer from an NTP such as ATP or GTP to any nucleoside diphosphate or its deoxy derivative. As NTPs, particularly GTP, are important for cellular macromolecular synthesis and signalling mechanisms, Ndk plays an important role in bacterial growth, signal transduction and pathogenicity. Specific examples of the role of Ndk in regulating growth, NTP formation and cell surface polysaccharide synthesis in two respiratory tract pathogens, Pseudomonas aeruginosa and Mycobacterium tuberculosis, are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1998.00846.x
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  • 2
    Electronic Resource
    Electronic Resource
    The BvgAS virulence control system regulates type III secretion in Bordetella bronchiseptica (1998)
    Oxford BSL : Blackwell Publishing Ltd
    Molecular microbiology 28 (1998), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The BvgAS signal transduction system in Bordetella spp. mediates a transition between infectious (Bvg+) and non-infectious (Bvg−) phases by sensing environmental conditions and regulating gene expression. Using differential display, arbitrary-primed polymerase chain reaction (PCR), we identified a gene expressed in the Bvg+ phase of Bordetella bronchiseptica that shows a high degree of sequence similarity to a locus involved in providing energy for type III secretion in pathogenic Gram-negative bacteria (yscN in Yersinia spp.). We determined that the expression of this homologue in B. bronchiseptica (designated bscN ) is regulated by bvg. Several open reading frames surrounding the bscN locus also show sequence similarity to loci encoding type III secretion apparatus components in other bacteria. An in-frame deletion of bscN in B. bronchiseptica leads to decreased secretion of several proteins, decreased cytotoxicity towards cultured cell lines and a defect in causing tyrosine dephosphorylation of specific proteins in infected cells in vitro. The deletion strain also revealed that bscN-mediated secretion is required for persistent colonization of the trachea in a rat infection model. Loci encoding type III secretion homologues were identified in four strains of B. pertussis and two strains of B. parapertussis. B. pertussis strain 18323 and an ovine isolate of B. parapertussis show significant transcription of the genes in vitro.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1998.00850.x
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  • 3
    Electronic Resource
    Electronic Resource
    Interplay between global regulators of Escherichia coli : effect of RpoS, Lrp and H-NS on transcription of the gene osmC (1998)
    Oxford BSL : Blackwell Publishing Ltd
    Molecular microbiology 28 (1998), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The transcription of the osmC gene of Escherichia coli is regulated as a function of the phase of growth. It is induced during the decelerating phase, before entry into stationary phase. osmC expression is directed by two overlapping promoters, osmCp1 and osmCp2. osmCp2 is mainly transcribed by E-σs, the RNA polymerase using the σs (RpoS) sigma factor, and is responsible for the growth phase regulation. Transcription from osmCp1 is independent of σs. The leucine-responsive protein (Lrp) has been shown to bind the osmC promoter region in band shift experiments. In vivo analysis using osmC–lacZ transcriptional fusions demonstrated that Lrp affects the expression of both promoters. It represses the transcription of osmCp1 and activates the transcription of osmCp2 by E-σs. An absence of Lrp results in an increase in the amount of RpoS during exponential growth in minimal medium. The nucleoid-associated protein H-NS also represses osmC transcription from both promoters. However, this happens through different mechanisms. The effect on osmCp2 is probably mediated by the increase in σs concentration in the cytoplasm of hns− mutants, while the effect on osmCp1 is independent of σs. No binding of H-NS to the promoter region DNA could be detected, indicating that the effect on osmCp1 could also be indirect.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1998.00855.x
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  • 4
    Electronic Resource
    Electronic Resource
    The structure of an ECF-σ-dependent, light-inducible promoter from the bacterium Myxococcus xanthus (1998)
    Oxford BSL : Blackwell Publishing Ltd
    Molecular microbiology 30 (1998), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Expression of the Myxococcus xanthus gene crtI is controlled by a light-inducible promoter. The activity of this promoter depends on CarQ, a σ factor of the extracytoplasmic function (ECF) subfamily. Here, we show that the minimum DNA stretch reproducing normal expression of crtI extends from a few bases upstream of the −35 position to a site well downstream of the transcriptional start. The downstream DNA contains an enhancer-like element that remains active when displaced upstream of the promoter. Experimental evidence is provided for the activity of the crtI promoter being critically dependent on a pentanucleotide sequence centred at the −31 position. The similarity of this sequence with the consensus for ECF-σ-dependent promoters from other bacteria is discussed. The activity of the crtI promoter also depends on certain basepairs at the −10 region. Hence, the operation of ECF-σ-factors seems to require binding to two different DNA sites, although the −10 sequences of different ECF-σ-dependent promoters are unrelated to one another, and the ECF-σ-factors themselves lack the conserved domain known to mediate binding of other σ-factors to the −10 DNA site.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1998.01129.x
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  • 5
    Electronic Resource
    Electronic Resource
    Pmt1 mannosyl transferase is involved in cell wall incorporation of several proteins in Saccharomyces cerevisiae (1998)
    Oxford BSL : Blackwell Publishing Ltd
    Molecular microbiology 27 (1998), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: We constructed hybrid proteins containing a plant α-galactosidase fused to various C-terminal moieties of the hypoxic Srp1p; this allowed us to identify a cell wall-bound form of Srp1p. We showed that the last 30 amino acids of Srp1p, but not the last 16, contain sufficient information to signal glycosyl-phosphatidylinositol anchor attachment and subsequent cell wall anchorage. The cell wall-bound form was shown to be linked by means of a β1,6-glucose-containing side-chain. Pmt1p enzyme is known as a protein-O-mannosyltransferase that initiates the O-glycosidic chains on proteins. We found that a pmt1 deletion mutant was highly sensitive to zymolyase and that in this strain the α-galactosidase–Srp1 fusion proteins, an α-galactosidase–Sed1 hybrid protein and an α-galactosidase–α-agglutinin hybrid protein were absent from both the membrane and the cell wall fractions. However, the plasma membrane protein Gas1p still receives its glycosyl-phosphatidylinositol anchor in pmt1 cells, and in this mutant strain an α-galactosidase–Cwp2 fusion protein was found linked to the cell wall but devoid of β1,6-glucan side-chain, indicating an alternative mechanism of cell wall anchorage.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1998.00660.x
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  • 6
    Electronic Resource
    Electronic Resource
    Differences in chromosome number and genome rearrangements in the genus Brucella (1998)
    Oxford BSL : Blackwell Publishing Ltd
    Molecular microbiology 27 (1998), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: We have studied the genomic structure and constructed the SpeI, PacI and I-CeuI restriction maps of the four biovars of the pathogenic bacterium Brucella suis. B. suis biovar 1 has two chromosomes of 2.1 Mb and 1.15 Mb, similar to those of the other Brucella species: B. melitensis, B. abortus, B. ovis and B. neotomae. Two chromosomes were also observed in the genome of B. suis biovars 2 and 4, but with sizes of 1.85 Mb and 1.35 Mb, whereas only one chromosome with a size of 3.1 Mb was found in B. suis biovar 3. We show that the differences in chromosome size and number can be explained by rearrangements at chromosomal regions containing the three rrn genes. The location and orientation of these genes confirmed that these rearrangements are due to homologous recombination at the rrn loci. This observation allows us to propose a scheme for the evolution of the genus Brucella in which the two chromosome-containing strains can emerge from an hypothetical ancestor with a single chromosome, which is probably similar to that of B. suis biovar 3. As the genus Brucella is certainly monospecific, this is the first time that differences in chromosome number have been observed in strains of the same bacterial species.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1998.00661.x
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  • 7
    Electronic Resource
    Electronic Resource
    A mechanical approach to the distribution and orientation of genes on genetic maps (1998)
    Oxford BSL : Blackwell Publishing Ltd
    Molecular microbiology 27 (1998), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1998.00669.x
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  • 8
    Electronic Resource
    Electronic Resource
    Isolation and analysis of xlnR, encoding a transcriptional activator co-ordinating xylanolytic expression in Aspergillus niger (1998)
    Oxford BSL : Blackwell Publishing Ltd
    Molecular microbiology 27 (1998), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Complementation by transformation of an Aspergillus niger mutant lacking xylanolytic activity led to the isolation of the xlnR gene. The xlnR gene encodes a polypeptide of 875 amino acids capable of forming a zinc binuclear cluster domain with similarity to the zinc clusters of the GAL4 superfamily of transcription factors. The XlnR-binding site 5′-GGCTAAA-3′ was deduced after electrophoretic mobility shift assays, DNase I footprinting and comparison of various xylanolytic promoters. The importance of the second G within the presumed XlnR binding site 5′-GGCTAAA-3′ was confirmed in vitro and in vivo. The 5′-GGCTAAA-3′ consensus sequence is found within several xylanolytic promoters of various Aspergillus species and Penicillium chrysogenum. Therefore, this sequence may be an important and conserved cis-acting element in induction of xylanolytic genes in filamentous fungi. Our results indicate that XlnR is a transcriptional activator of the xylanolytic system in A. niger.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1998.00666.x
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  • 9
    Electronic Resource
    Electronic Resource
    Distinct regions of the colicin A translocation domain are involved in the interaction with TolA and TolB proteins upon import into Escherichia coli (1998)
    Oxford BSL : Blackwell Publishing Ltd
    Molecular microbiology 27 (1998), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Group A colicins need proteins of the Escherichia coli envelope Tol complex (TolA, TolB, TolQ and TolR) to reach their cellular target. The N-terminal domain of colicins is involved in the import process. The N-terminal domains of colicins A and E1 have been shown to interact with TolA, and the N-terminal domain of colicin E3 has been shown to interact with TolB. We found that a pentapeptide conserved in the N-terminal domain of all group A colicins, the ‘TolA box’, was important for colicin A import but was not involved in the colicin A–TolA interaction. It was, however, involved in the colicin A–TolB interaction. The interactions of colicin A N-terminal domain deletion mutants with TolA and TolB were investigated. Random mutagenesis was performed on a construct allowing the colicin A N-terminal domain to be exported in the bacteria periplasm. This enabled us to select mutant protein domains unable to compete with the wild-type domain of the entire colicin A for import into the cells. Our results demonstrate that different regions of the colicin A N-terminal domain interact with TolA and TolB. The colicin A N-terminal domain was also shown to form a trimeric complex with TolA and TolB.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1998.00667.x
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  • 10
    Electronic Resource
    Electronic Resource
    RNase T is related to dnaQ and family C DNA polymerases (1998)
    Oxford BSL : Blackwell Publishing Ltd
    Molecular microbiology 27 (1998), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1998.00673.x
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