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Gene Review

ECs4527  -  ATP-dependent DNA helicase RecG

Escherichia coli O157:H7 str. Sakai

 
 
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Disease relevance of ECs4527

  • The RecG protein of E. coli is a junction-specific DNA helicase involved in recombination and DNA repair [1].
  • The mmsA locus of Streptococcus pneumoniae encodes a RecG-like protein involved in DNA repair and in three-strand recombination [2].
  • These results suggest that in addition to RecBCD enzyme, RuvABC and RecG proteins are also involved in the inhibition of prophage recombinogenicity [3].
  • We purified RecG proteins from three other species: two Gram-positive mesophiles, Bacillus subtilis and Streptococcus pneumoniae, and one extreme thermophile, Aquifex aeolicus [4].
 

High impact information on ECs4527

  • The role of RecG provides novel insights into the interplay between transcription, replication, and recombination, and suggests a general model in which recombination underpins genome duplication in the face of frequent obstacles to replication fork progression [5].
  • Reverse branch migration of Holliday junctions by RecG protein: a new mechanism for resolution of intermediates in recombination and DNA repair [1].
  • We suggest that the RecG mechanism for resolution of junctions is universal and provides a simple system that allows gene conversion without associated crossing over [1].
  • Direct rescue of stalled DNA replication forks via the combined action of PriA and RecG helicase activities [6].
  • We found that overproduction of RecG protein drastically decreased copy numbers of ColE1-type plasmids, which require R-loop formation between the template DNA and a primer RNA transcript (RNA II) for the initiation of replication [7].
 

Chemical compound and disease context of ECs4527

 

Biological context of ECs4527

  • A step backward in advancing DNA replication: rescue of stalled replication forks by RecG [9].
  • These results suggest that overproduced RecG inhibits the initiation of replication by prematurely resolving the R-loops formed at the replication origin region of these plasmids with its unique helicase activity [7].
  • ATP-dependent resolution of R-loops at the ColE1 replication origin by Escherichia coli RecG protein, a Holliday junction-specific helicase [7].
  • The RecG protein of Escherichia coli is a junction-specific DNA helicase that drives branch migration of Holliday intermediates in genetic recombination and DNA repair [10].
  • RecG dissociates X-junctions to flayed duplex products, although DNA unwinding of the heterologous arms is limited to </=30 base pairs [10].
 

Associations of ECs4527 with chemical compounds

  • These inhibitory effects are not mediated specifically by Mg2+; e.g. both Ca2+ and hexamminecobalt(III) chloride also inhibit X-junction binding and unwinding by RecG [10].
  • To begin to assign structure-function relationships within RecG, a series of N- and C-terminal deletions have been engineered into the protein, together with an N-terminal histidine tag fusion peptide for purification purposes [11].
  • The involvement of the LexA-controlled RuvAB and RecA proteins with the RecG and RecBCD proteins in metabolism and cell viability implies that DNA double-strand breaks (DSB), and thus hydroxyl radicals that normally generate this type of damage, are produced in Pi-starved cells [12].
 

Analytical, diagnostic and therapeutic context of ECs4527

  • Using electron microscopy and gel electrophoresis, we demonstrate that another protein, E. coli RecG helicase, promotes extensive fork regression in the same system [13].
  • We have found that RecG exists as a monomer in solution as measured by gel filtration but when bound to junction DNA the enzyme forms two distinct protein-DNA complexes that contain one and two protein molecules [14].

References

  1. Reverse branch migration of Holliday junctions by RecG protein: a new mechanism for resolution of intermediates in recombination and DNA repair. Whitby, M.C., Ryder, L., Lloyd, R.G. Cell (1993) [Pubmed]
  2. The mmsA locus of Streptococcus pneumoniae encodes a RecG-like protein involved in DNA repair and in three-strand recombination. Martin, B., Sharples, G.J., Humbert, O., Lloyd, R.G., Claverys, J.P. Mol. Microbiol. (1996) [Pubmed]
  3. Loss of lambda prophage recombinogenicity in UV-irradiated Escherichia coli: the role of host genes ruvA, ruvB, ruvC, and recG. Zahradka, K., Zahradka, D., Petranović, M. Res. Microbiol. (2001) [Pubmed]
  4. Conservation of RecG activity from pathogens to hyperthermophiles. Wen, Q., Mahdi, A.A., Briggs, G.S., Sharples, G.J., Lloyd, R.G. DNA Repair (Amst.) (2005) [Pubmed]
  5. Modulation of RNA polymerase by (p)ppGpp reveals a RecG-dependent mechanism for replication fork progression. McGlynn, P., Lloyd, R.G. Cell (2000) [Pubmed]
  6. Direct rescue of stalled DNA replication forks via the combined action of PriA and RecG helicase activities. Gregg, A.V., McGlynn, P., Jaktaji, R.P., Lloyd, R.G. Mol. Cell (2002) [Pubmed]
  7. ATP-dependent resolution of R-loops at the ColE1 replication origin by Escherichia coli RecG protein, a Holliday junction-specific helicase. Fukuoh, A., Iwasaki, H., Ishioka, K., Shinagawa, H. EMBO J. (1997) [Pubmed]
  8. RecN and RecG are required for Escherichia coli survival of Bleomycin-induced damage. Kosa, J.L., Zdraveski, Z.Z., Currier, S., Marinus, M.G., Essigmann, J.M. Mutat. Res. (2004) [Pubmed]
  9. A step backward in advancing DNA replication: rescue of stalled replication forks by RecG. Dillingham, M.S., Kowalczykowski, S.C. Mol. Cell (2001) [Pubmed]
  10. Targeting Holliday junctions by the RecG branch migration protein of Escherichia coli. Whitby, M.C., Lloyd, R.G. J. Biol. Chem. (1998) [Pubmed]
  11. DNA binding and helicase domains of the Escherichia coli recombination protein RecG. Mahdi, A.A., McGlynn, P., Levett, S.D., Lloyd, R.G. Nucleic Acids Res. (1997) [Pubmed]
  12. Role of Escherichia coli RpoS, LexA and H-NS global regulators in metabolism and survival under aerobic, phosphate-starvation conditions. Gérard, F., Dri, A.M., Moreau, P.L. Microbiology (Reading, Engl.) (1999) [Pubmed]
  13. Situational repair of replication forks: roles of RecG and RecA proteins. Robu, M.E., Inman, R.B., Cox, M.M. J. Biol. Chem. (2004) [Pubmed]
  14. Characterisation of the catalytically active form of RecG helicase. McGlynn, P., Mahdi, A.A., Lloyd, R.G. Nucleic Acids Res. (2000) [Pubmed]
 
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