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  • Protein-protein interactions  (2)
  • uvp1 gene  (1)
  • 1
    ISSN: 1617-4623
    Keywords: Key words R46 plasmid ; uvp1 gene ; Resolvase ; Site-specific recombination ; Integron
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The product of the uvp1 gene of the R46 plasmid, a member of the DNA invertase-resolvase family, was studied to characterize its recombination activity on the R46 plasmid. The purified Uvp1 protein specifically binds to a 256-bp DNA fragment located immediately upstream of the uvp1 gene itself, and overlapping the 5′-conserved segment (5′-CS) of the R46 integron In1. We identified on this fragment a putative resolution (res) site. Using an in vitro assay, we demonstrated the ability of the protein to resolve a synthetic cointegrate containing a direct repeat of the res site. In vivo, we obtained cointegrate resolution in Uvp1-expressing recA − cells. Sites I and II, subsites of the putative res site, lie within the outer boundary of the integron 5′-CS which is common to all the known integrons. Furthermore, a 69-bp DNA element (containing site I) is required for cointegrate resolution. We propose that this recombination mechanism protects R46 plasmid against unequal distribution following fusion with either identical or different integron-bearing plasmids. Moreover, Uvp1 might have a role in generating gene cassette diversity between the two conserved segments of the integron.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1617-4623
    Keywords: Key words Drosophila ; Enhancer of split ; achaete-scute ; Helix-loop-helix proteins ; Protein-protein interactions
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  The Enhancer of split and achaete-scute gene complexes [E(spl)-C and AS-C] encode helix-loophelix proteins required for neurogenesis in Drosophila. Using a heterologous bacterial system, we show that (i) the bHLH domains of the proteins encoded by the two gene complexes differ in their ability to form homo- and/or heterodimers; (ii) the bHLH domains of the E(spl)-C proteins m5, m7 and m8 interact with the bHLH domains of the Ac and Sc proteins. These bHLH domains form an interaction network which may represent the molecular mechanism whereby the competent state of the proneural cells is maintained until the terminal determination to neuroblast occurs. Also, the pattern of interactions of the bHLH domains of certain proteins encoded by the two gene complexes may explain their functional redundancy.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1617-4623
    Keywords: Drosophila ; Enhancer of split ; achaete-scute ; Helix-loop-helix proteins ; Protein-protein interactions
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract TheEnhancer of split andachaete-scute gene complexes [E(spl)-C and AS-C] encode helix-loop-helix proteins required for neurogenesis inDrosophila. Using a heterologous bacterial system, we show that (i) the bHLH domains of the proteins encoded by the two gene complexes differ in their ability to form homo- and/or heterodimers; (ii) the bHLH domains of the E(spl)-C proteins m5, m7 and m8 interact with the bHLH domains of the Ac and Sc proteins. These bHLH domains form an interaction network which may represent the molecular mechanism whereby the competent state of the proneural cells is maintained until the terminal determination to neuroblast occurs. Also, the pattern of interactions of the bHLH domains of certain proteins encoded by the two gene complexes may explain their functional redundancy.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
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