[Enzymatic control of homologous recombination in Escherichia coli cells and hyper-recombination].

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  • Author(s): Bakhlanova IV; Dudkina AV; Baĭtin DM
  • Source:
    Molekuliarnaia biologiia [Mol Biol (Mosk)] 2013 Mar-Apr; Vol. 47 (2), pp. 205-17.
  • Publication Type:
    Journal Article; Review
  • Language:
    Russian
  • Additional Information
    • Source:
      Publisher: Izdatelstvo Nauka Country of Publication: Russia (Federation) NLM ID: 0105454 Publication Model: Print Cited Medium: Print ISSN: 0026-8984 (Print) Linking ISSN: 00268984 NLM ISO Abbreviation: Mol Biol (Mosk) Subsets: MEDLINE
    • Publication Information:
      Original Publication: Moskva : Izdatelstvo Nauka
    • Subject Terms:
      Escherichia coli/*enzymology ; Homologous Recombination/*genetics ; Rec A Recombinases/*genetics; DNA, Single-Stranded/genetics ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Escherichia coli/genetics ; Escherichia coli/radiation effects ; Gamma Rays ; Gene Expression Regulation, Bacterial ; Gene Expression Regulation, Enzymologic ; Homologous Recombination/radiation effects ; Rec A Recombinases/metabolism ; Ultraviolet Rays
    • Abstract:
      The RecA protein is a major enzyme of homologous recombination in bacterial cell. Forming a right-handed helical filament on ssDNA, it provides a homology search between two DNA molecules and homologous strand exchange. The RecA protein not only defends the cell from exposure to ionizing radiation and UV-irradiation, but also ensures the recombination process in the course of normal cell growth. A number of wild-type or mutant RecA proteins demonstrate increased recombinogenic properties in vitro and in vivo as compared with the wild-type RecA protein from Escherichia coli, which leads to hyper-recombination. The hyper-rec activity of RecA proteins during the recombination process in many depends on the filamentation dynamics on ssDNA and DNA-transferase properties. Changes in filamentation and DNA-transferase abilities of RecA protein may be the result of not only specific amino-acid substitutions, but also the functioning of the cell enzymatic apparatus, including such proteins as RecO, RecR, RecF, RecX, DinI, SSB, PsiB. To date, the function of each of these proteins is identified at the molecular level. However, the role of some of them in the cell metabolism remains to be seen. Increase in recombination in vivo is not always useful for a cell and faces various limitations. Moreover, in the bacterial cell some mechanisms are activated, that cause genomic reorganization, directed to suppress the expression of hyper-active RecA protein. The ways of hyper-active RecA protein regulation are very interesting, and they are studied in different model systems.
    • Accession Number:
      0 (DNA, Single-Stranded)
      0 (DNA-Binding Proteins)
      EC 2.7.7.- (Rec A Recombinases)
    • Publication Date:
      Date Created: 20130702 Date Completed: 20130805 Latest Revision: 20201209
    • Publication Date:
      20231215
    • Accession Number:
      10.7868/s0026898413020031
    • Accession Number:
      23808153