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  • 1
    Digitale Medien
    Digitale Medien
    Reaction of the antitumor antibiotic CC-1065 with DNA. Location of the site of thermally induced strand breakage and analysis of DNA sequence specificity (1985)
    s.l. : American Chemical Society
    Biochemistry 24 (1985), S. 6228-6237 
    Details
    ISSN: 1520-4995
    Quelle: ACS Legacy Archives
    Thema: Biologie , Chemie und Pharmazie
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1021/bi00343a029
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  • 2
    Digitale Medien
    Digitale Medien
    DNA sequence specificity of the pyrrolo[1,4]benzodiazepine antitumor antibiotics. Methidiumpropyl-EDTA-iron(II) footprinting analysis of DNA binding sites for anthramycin and related drugs (1986)
    s.l. : American Chemical Society
    Biochemistry 25 (1986), S. 1249-1258 
    Details
    ISSN: 1520-4995
    Quelle: ACS Legacy Archives
    Thema: Biologie , Chemie und Pharmazie
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1021/bi00354a009
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  • 3
    Digitale Medien
    Digitale Medien
    No syringes please, ejection of phage T7 DNA from the virion is enzyme driven (2001)
    Oxford, UK : Blackwell Science, Ltd
    Molecular microbiology 40 (2001), S. 0 
    Details
    ISSN: 1365-2958
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie , Medizin
    Notizen: Development of a sensitive assay that measures the rate of cellular internalization of an infecting bacteriophage T7 genome has led to surprising observations on the initiation of infection. Proteins ejected from the phage virion probably function as an extensible tail to form a channel across the cell envelope. This channel is subsequently used for translocating the phage genome into the cell. One of these ejected proteins also controls the amount of DNA that enters the cell, rendering subsequent internalization of the remainder of the genome dependent on transcription. Mutations affecting this protein allow the entire phage genome to enter a cell by the transcription-independent process. This process exhibits pseudo-zero-order reaction kinetics and a temperature dependence of translocation rate that are not expected if DNA ejection from a phage capsid were caused by a physical process. The temperature dependence of transcription-independent T7 DNA translocation rate is similar to those of enzyme-catalysed reactions. Current data suggest a highly speculative model, in which two of the proteins ejected from the phage head establish a molecular motor that ratchets the phage genome into the cell.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1046/j.1365-2958.2001.02357.x
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  • 4
    Digitale Medien
    Digitale Medien
    Role of the Gp16 lytic transglycosylase motif in bacteriophage T7 virions at the initiation of infection (2000)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 37 (2000), S. 0 
    Details
    ISSN: 1365-2958
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie , Medizin
    Notizen: The predicted catalytic glutamate residue for transglycosylase activity of bacteriophage T7 gp16 is not essential for phage growth, but is shown to be beneficial during infection of Escherichia coli cells grown to high cell density, conditions in which murein is more highly cross-linked. In the absence of the putative transglycosylase, internalization of the phage genome is significantly delayed during infection. The lytic transglycosylase motif of gp16 is essential for phage growth at temperatures below 20°C, indicating that these growth conditions also lead to increased cross-linking of peptidoglycan. Overexpression of sltY, E. coli soluble lytic transglycosylase, partially complements the defect in infection of mutant phage particles, allowing them to infect at higher efficiencies. Conversely, an sltY deletion increases the latent period of wild-type phage.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1046/j.1365-2958.2000.01995.x
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  • 5
    Digitale Medien
    Digitale Medien
    Bacteriophage T7 DNA ejection into cells is initiated by an enzyme-like mechanism (2004)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 53 (2004), S. 0 
    Details
    ISSN: 1365-2958
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie , Medizin
    Notizen: In a normal infection about 850 bp of the bacteriophage T7 genome is ejected into the cell, the remainder of the genome is internalized through transcription by Escherichia coli and then T7 RNA polymerase. Rates of T7 DNA internalization by the E. coli enzyme in vivo are constant across the whole genome. As expected for an enzyme-catalysed reaction, rates vary with temperature and can be fitted to Arrhenius kinetics. Phage virions containing a mutant gp16, a protein known to be ejected from the phage capsid into the cell at the initiation of infection, allow complete entry of the T7 genome in the absence of transcription. The kinetics of DNA ejection from such a mutant virion into the bacterial cytoplasm have also been measured at different temperatures in vivo. Between 15 and 43°C the entire 40 kb T7 genome is translocated into the cell at a constant rate that is characteristic for each temperature, and the temperature-dependence of DNA translocation rates can be fitted to Arrhenius kinetics. The data are consistent with the idea that transcription-independent DNA translocation from the T7 virion is also enzyme-catalysed. The proton motive force is necessary for this mode of DNA translocation, because collapsing the membrane potential while the T7 genome is entering the cell abruptly halts further DNA transfer.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1365-2958.2004.04204.x
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  • 6
    Digitale Medien
    Digitale Medien
    Peptidoglycan hydrolytic activities associated with bacteriophage virions (2004)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 51 (2004), S. 0 
    Details
    ISSN: 1365-2958
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie , Medizin
    Notizen: Murein hydrolases appear to be widespread in the virions of bacteriophages infecting Gram-positive or Gram-negative bacteria. Muralytic activity has been found in virions of the majority of a diverse collection of phages. Where known, the enzyme is either part of a large protein or found associated with other structural components of the virion that limit enzyme activity. In most cases, the lack of genetic and structural characterization of the phage precludes making a definitive identification of the enzymatic protein species. However, three proteins with muralytic activity have been unequivocally identified. T7gp16 is a 144 kDa internal head protein that is ejected into the cell at the initiation of infection; its enzyme activity is required only when the cell wall is more highly cross-linked. P22gp4 is part of the neck of the particle and is essential for infectivity. The activity associated with virions of Bacillus subtilis phage ø29 and its relatives lies in the terminal protein gp3. These studies lead to a general mechanism describing how phage genomes are transported across the bacterial cell wall.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1046/j.1365-2958.2003.03894.x
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  • 7
    Digitale Medien
    Digitale Medien
    A novel mutant of bacteriophage T7 that is defective in early phage DNA synthesis (1980)
    Springer
    Molecular genetics and genomics 179 (1980), S. 683-691 
    Details
    ISSN: 1617-4623
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Summary A mutant of bacteriophage T7 is described which produces smaller plaques than the wild type and is defective in early phage DNA synthesis. The mutation is located in the Class II transcriptional region of the T7 genome together with all the other genes involved in phage DNA synthesis, but it could not be placed into any of the existing known T7 genes. DNA replication in strain R9 begins at the same time as for wild type although it proceeds very slowly until 15 minutes after infection, after which time DNA synthesis is apparently normal. It is concluded therefore that there are two types of DNA replication in phage T7, which differ with respect to their dependence on the mutant function. The change from one mode to the other is marked by the formation of folded, complex DNA inside the cell.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00271758
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  • 8
    Digitale Medien
    Digitale Medien
    Preliminary molecular replacement results for a crystalline gene 5 protein-deoxyoligonucleotide complex (1979)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 10 (1979), S. 479-489 
    Details
    ISSN: 0091-7419
    Schlagwort(e): protein-nucleic acid interactions ; X-ray diffraction ; gene 5 protein ; molecular replacement ; DNA ; fd bacteriophage ; Life Sciences ; Molecular Cell Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Chemie und Pharmazie , Medizin
    Notizen: Complexes of the gene 5 protein from bacteriophage fd with a variety of oligodeoxynucleotides, ranging in length from two to eight and comprised of several different sequences, have been formed and crystallized for X-ray diffraction analysis. The crystallographic parameters of four different unit cells, all of which are based on hexagonal packing arrangements, indicate that the fundamental unit of the complex is composed of six gene 5 protein dimers. We believe this aggregate has 622 point group symmetry and is a ring formed by end-to-end closure of a linear array of six dimers. From our results we have proposed a double-helix model for the gene 5 protein-DNA complex in which the protein forms a spindle or core around which the DNA is spooled. Currently 5.0-Å X-ray diffraction data from one of the crystalline complexes is being analyzed by molecular replacement techniques to obtain a direct image of the protein-nucleic acid complex.
    Zusätzliches Material: 6 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/jss.400100410
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  • 9
    Digitale Medien
    Digitale Medien
    Structure of the dna binding cleft of the gene 5 protein from bacteriophage fd (1979)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 10 (1979), S. 457-465 
    Details
    ISSN: 0091-7419
    Schlagwort(e): DNA binding protein ; gene 5 ; fd bacteriophage ; X-ray diffraction ; protein-nucleic acid interactions ; Life Sciences ; Molecular Cell Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Chemie und Pharmazie , Medizin
    Notizen: The structure of the gene 5 DNA unwinding protein from bacteriophage fd has been solved to 2.3-Å resolution by X-ray diffraction techniques. The molecule contains an extensive cleft region that we have identified as the DNA binding site on the basis of the residues that comprise its surface. The interior of the groove has a rather large number of basic amino acid residues that serve to draw the polynucleotide backbone into the cleft. Arrayed along the external edges of the groove are a number of aromatic amino acid side groups that are in position to stack upon the bases of the DNA and fix it in place. The structure and binding mechanism as we visualize it appear to be fully consistent with evidence provided by physical-chemical studies of the protein in solution.
    Zusätzliches Material: 6 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/jss.400100408
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