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  • Articles: DFG German National Licenses  (2)
  • DNA-binding protein  (2)
  • 1
    ISSN: 1617-4623
    Keywords: DNA curvature ; DNA-binding protein ; σs-dependent expressionEscherichia coli
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract FromEscherichia coli, a DNA-binding protein that preferentially recognizes a curved DNA sequence was isolated and shown to correspond to one that has recently been reported as a binding protein for the replication origin of theE. coli chromosome, named Rob. Here, arob promoter-lacZ transcriptional fusion was constructed on the chromosome, and used to demonstrate that the expression ofrob is notably enhanced at the onset of stationary phase in Luria-broth and also under certain growth conditions in a minimal medium, such as glucose- and phosphate-starvation medium. It was further shown that this growth condition-dependent expression ofrob is notably reduced in a null mutant for the stationary phase-specific sigma subunit of RNA polymerase, σs, although σs-independent expression ofrob was significant during the logarithmic growth phase. Furthermore therob null mutant was found to exhibit, as compared with the wild-type, an altered profile of protein synthesis, particularly at the very late stationary phase.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0749-503X
    Keywords: Fission yeast ; DNA curvature ; gel shift assay ; DNA-binding protein ; cloning and sequencing ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We searched for fission yeast (Schizosaccharomyces pombe) proteins that preferentially bind to a synthetic curved DNA sequence, by means of a DNA-binding gel shift assay in the presence of an excess amount of a non-curved DNA sequence as a competitor. We identified such a protein in S. pombe. The protein, thus purified, has an apparent molecular weight of 42 000, as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. It was suggested that this protein (42 K-protein) recognizes and binds to a curved DNA structure in a given nucleotide sequence, although it also binds to a non-curved DNA sequence with lower affinity. As its putative coding sequence, a 1·9-kilobase genomic DNA from S. pombe was cloned and sequenced. Sequencing of a cDNA clone also revealed the existence of an open reading frame, with no intron, encoding a 381-amino-acid protein with a calculated molecular mass, 41 597. This protein appears to be located in the nucleus. The predicted protein sequence revealed that the 42 K-protein exhibits no significant similarity to any other known proteins, except to a hypothetical protein of Caenorhabditis elegans.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
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