Site-specific recombination by phiC31 integrase and other large serine recombinases.

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  • Author(s): Smith MC;Smith MC; Brown WR; McEwan AR; Rowley PA
  • Source:
    Biochemical Society transactions [Biochem Soc Trans] 2010 Apr; Vol. 38 (2), pp. 388-94.
  • Publication Type:
    Journal Article; Research Support, Non-U.S. Gov't; Review
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Portland Press On The Behalf Of The Biochemical Society Country of Publication: England NLM ID: 7506897 Publication Model: Print Cited Medium: Internet ISSN: 1470-8752 (Electronic) Linking ISSN: 03005127 NLM ISO Abbreviation: Biochem Soc Trans Subsets: MEDLINE
    • Publication Information:
      Original Publication: London : Portland Press On The Behalf Of The Biochemical Society
    • Subject Terms:
      Bacteriophages/*enzymology ; Integrases/*metabolism ; Recombinases/*metabolism ; Recombination, Genetic/*physiology; Bacteriophages/genetics ; Bacteriophages/metabolism ; Catalytic Domain ; Integrases/chemistry ; Integrases/physiology ; Models, Biological ; Molecular Weight ; Recombinases/chemistry ; Recombinases/physiology ; Serine/metabolism ; Substrate Specificity
    • Abstract:
      Most temperate phages encode an integrase for integration and excision of the prophage. Integrases belong either to the lambda Int family of tyrosine recombinases or to a subgroup of the serine recombinases, the large serine recombinases. Integration by purified serine integrases occurs efficiently in vitro in the presence of their cognate (~50 bp) phage and host attachment sites, attP and attB respectively. Serine integrases require an accessory protein, Xis, to promote excision, a reaction in which the products of the integration reaction, attL and attR, recombine to regenerate attP and attB. Unlike other directional recombinases, serine integrases are not controlled by proteins occupying accessory DNA-binding sites. Instead, it is thought that different integrase conformations, induced by binding to the DNA substrates, control protein-protein interactions, which in turn determine whether recombination proceeds. The present review brings together the evidence for this model derived from the studies on phiC31 integrase, Bxb1 integrase and other related proteins.
    • Number of References:
      60
    • Grant Information:
      BB/H001212/1 United Kingdom BB_ Biotechnology and Biological Sciences Research Council; BB/E000894/1 United Kingdom BB_ Biotechnology and Biological Sciences Research Council; BB/D007836/1 United Kingdom BB_ Biotechnology and Biological Sciences Research Council
    • Accession Number:
      0 (Recombinases)
      452VLY9402 (Serine)
      EC 2.7.7.- (Integrases)
    • Publication Date:
      Date Created: 20100320 Date Completed: 20100611 Latest Revision: 20220129
    • Publication Date:
      20231215
    • Accession Number:
      10.1042/BST0380388
    • Accession Number:
      20298189