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Gene Review

pO157p22  -  recombinase

Escherichia coli O157:H7 str. Sakai

 
 
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Disease relevance of pO157p22

  • They include the 21,000 dalton recombinase (Hin), a 12,000 dalton host protein (Factor II), and one of the major histone-like proteins of E. coli HU [1].
  • Bacteriophage P1 encodes its own site-specific recombination system consisting of a site at which recombination takes place called loxP and a recombinase called Cre [2].
  • The predicted XisF protein shows significant similarity to the Bacillus subtilis SpoIVCA recombinase [3].
  • The Hin recombinase of Salmonella normally catalyzes a site-specific DNA inversion reaction that is very efficient when the Fis protein and a recombinational enhancer sequence are present [4].
  • Helper viruses were constructed with packaging signals flanked by loxP sites so that in 293 cells that stably express the Cre recombinase (293Cre), the packaging signal was efficiently excised, rendering the helper virus genome unpackageable [5].
 

High impact information on pO157p22

  • During lambda integration, Int recombinase must specifically bind to and cut attachment sites on both the viral and host chromosomes [6].
  • During site-specific DNA recombination, which brings about genetic rearrangement in processes such as viral integration and excision and chromosomal segregation, recombinase enzymes recognize specific DNA sequences and catalyse the reciprocal exchange of DNA strands between these sites [7].
  • The data support a model in which C-terminal intersubunit interactions contribute to coupled protein-DNA conformational changes that lead to sequential activation and reciprocal inhibition of pairs of active sites in the recombinase tetramer during recombination [8].
  • Recombination reactions using XerC and XerD derivatives that are mutant in their presumptive catalytic residues, or are maltose-binding fusion recombinase derivatives, have demonstrated that this pair of strand exchanges is catalysed by XerC [9].
  • This unique association between the integrase-like TnpI recombinase and the TnpA transposase qualifies Tn4430 as a member of a new group within the class II mobile genetic elements [10].
 

Chemical compound and disease context of pO157p22

 

Biological context of pO157p22

 

Anatomical context of pO157p22

 

Associations of pO157p22 with chemical compounds

  • The arginine residue at position 308 in the Flp recombinase corresponds to the only invariant arginine within the Int family of recombinases [25].
  • Changing Leu-43 to lysine abolishes the NaeI endonuclease activity and replaces it with topoisomerase and recombinase activities [26].
  • The switch lies immediately downstream from the fimE gene, coding for a tyrosine site-specific recombinase that catalyses inversion of the switch from the ON to the OFF phase [27].
  • This effect is seen only when phosphorothioate is positioned at a point of potential cleavage by Int recombinase, demonstrating that the inhibition of strand exchange is highly specific [28].
  • The positions and characteristics of the mutations support a mechanism for strand exchange by serine recombinases in which the DNA is on the outside of a recombinase tetramer, and the tertiary/quaternary structure of the tetramer is reconfigured [29].
 

Other interactions of pO157p22

  • NaeI, a novel DNA endonuclease, shows topoisomerase and recombinase activities when a Lys residue is substituted for Leu 43 [30].
  • Like its parent, the resulting plasmid, pAW800, undergoes complex multiple DNA inversions: this DNA inversion system is therefore called Min. The min gene, which codes for the p15B Min DNA invertase, can complement the P1 cin recombinase gene [31].
  • Complementation tests have indicated that both the 5'-->3' exonuclease and the polymerization activities of DNA polymerase I are essential for viability in the absence of RecA protein, whereas the viability and DNA replication of DNA polymerase I-defective cells depend on the recombinase activity of RecA [32].
 

Analytical, diagnostic and therapeutic context of pO157p22

References

  1. Host protein requirements for in vitro site-specific DNA inversion. Johnson, R.C., Bruist, M.F., Simon, M.I. Cell (1986) [Pubmed]
  2. Studies on the properties of P1 site-specific recombination: evidence for topologically unlinked products following recombination. Abremski, K., Hoess, R., Sternberg, N. Cell (1983) [Pubmed]
  3. Anabaena xisF gene encodes a developmentally regulated site-specific recombinase. Carrasco, C.D., Ramaswamy, K.S., Ramasubramanian, T.S., Golden, J.W. Genes Dev. (1994) [Pubmed]
  4. Configuration of DNA strands and mechanism of strand exchange in the Hin invertasome as revealed by analysis of recombinant knots. Heichman, K.A., Moskowitz, I.P., Johnson, R.C. Genes Dev. (1991) [Pubmed]
  5. A helper-dependent adenovirus vector system: removal of helper virus by Cre-mediated excision of the viral packaging signal. Parks, R.J., Chen, L., Anton, M., Sankar, U., Rudnicki, M.A., Graham, F.L. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  6. Synapsis of attachment sites during lambda integrative recombination involves capture of a naked DNA by a protein-DNA complex. Richet, E., Abcarian, P., Nash, H.A. Cell (1988) [Pubmed]
  7. Structure of Cre recombinase complexed with DNA in a site-specific recombination synapse. Guo, F., Gopaul, D.N., van Duyne, G.D. Nature (1997) [Pubmed]
  8. Reciprocal control of catalysis by the tyrosine recombinases XerC and XerD: an enzymatic switch in site-specific recombination. Hallet, B., Arciszewska, L.K., Sherratt, D.J. Mol. Cell (1999) [Pubmed]
  9. Xer site-specific recombination in vitro. Arciszewska, L.K., Sherratt, D.J. EMBO J. (1995) [Pubmed]
  10. Structural and functional analysis of Tn4430: identification of an integrase-like protein involved in the co-integrate-resolution process. Mahillon, J., Lereclus, D. EMBO J. (1988) [Pubmed]
  11. Selective disruption of genes transiently induced in differentiating mouse embryonic stem cells by using gene trap mutagenesis and site-specific recombination. Thorey, I.S., Muth, K., Russ, A.P., Otte, J., Reffelmann, A., von Melchner, H. Mol. Cell. Biol. (1998) [Pubmed]
  12. Tyr60 variants of Flp recombinase generate conformationally altered protein-DNA complexes. Differential activity in full-site and half-site recombinations. Chen, J.W., Evans, B.R., Zheng, L., Jayaram, M. J. Mol. Biol. (1991) [Pubmed]
  13. Sequence-specific covalent modification of DNA by cross-linking oligonucleotides. Catalysis by RecA and implication for the mechanism of synaptic joint formation. Podyminogin, M.A., Meyer, R.B., Gamper, H.B. Biochemistry (1995) [Pubmed]
  14. Escherichia coli RecA promotes strand invasion with cisplatin-damaged DNA. Nimonkar, A.V., Le Gac, N.T., Villani, G., Boehmer, P.E. Biochimie (2006) [Pubmed]
  15. Analysis of the lambdoid prophage element e14 in the E. coli K-12 genome. Mehta, P., Casjens, S., Krishnaswamy, S. BMC Microbiol. (2004) [Pubmed]
  16. Antagonistic controls regulate copy number of the yeast 2 mu plasmid. Murray, J.A., Scarpa, M., Rossi, N., Cesareni, G. EMBO J. (1987) [Pubmed]
  17. Nerve growth factor somatic mosaicism produced by herpes virus-directed expression of cre recombinase. Brooks, A.I., Muhkerjee, B., Panahian, N., Cory-Slechta, D., Federoff, H.J. Nat. Biotechnol. (1997) [Pubmed]
  18. Improved properties of FLP recombinase evolved by cycling mutagenesis. Buchholz, F., Angrand, P.O., Stewart, A.F. Nat. Biotechnol. (1998) [Pubmed]
  19. Chimeric recombinases with designed DNA sequence recognition. Akopian, A., He, J., Boocock, M.R., Stark, W.M. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  20. Detection of anti-type 3 muscarinic acetylcholine receptor autoantibodies in the sera of Sjögren's syndrome patients by use of a transfected cell line assay. Gao, J., Cha, S., Jonsson, R., Opalko, J., Peck, A.B. Arthritis Rheum. (2004) [Pubmed]
  21. Plastid marker-gene excision by transiently expressed CRE recombinase. Lutz, K.A., Bosacchi, M.H., Maliga, P. Plant J. (2006) [Pubmed]
  22. Construction of an excisable bacterial artificial chromosome containing a full-length infectious clone of herpes simplex virus type 1: viruses reconstituted from the clone exhibit wild-type properties in vitro and in vivo. Tanaka, M., Kagawa, H., Yamanashi, Y., Sata, T., Kawaguchi, Y. J. Virol. (2003) [Pubmed]
  23. Targeting mammary epithelial cells using a bacterial artificial chromosome. Wintermantel, T.M., Mayer, A.K., Schütz, G., Greiner, E.F. Genesis (2002) [Pubmed]
  24. Genomic targeting with an MBP-Cre fusion protein. Kolb, A.F., Siddell, S.G. Gene (1996) [Pubmed]
  25. Functional analysis of Arg-308 mutants of Flp recombinase. Possible role of Arg-308 in coupling substrate binding to catalysis. Parsons, R.L., Evans, B.R., Zheng, L., Jayaram, M. J. Biol. Chem. (1990) [Pubmed]
  26. Amino acid substitutions at position 43 of NaeI endonuclease. Evidence for changes in NaeI structure. Carrick, K.L., Topal, M.D. J. Biol. Chem. (2003) [Pubmed]
  27. A Rho-dependent phase-variable transcription terminator controls expression of the FimE recombinase in Escherichia coli. Joyce, S.A., Dorman, C.J. Mol. Microbiol. (2002) [Pubmed]
  28. An intermediate in the phage lambda site-specific recombination reaction is revealed by phosphorothioate substitution in DNA. Kitts, P.A., Nash, H.A. Nucleic Acids Res. (1988) [Pubmed]
  29. Activating mutations of Tn3 resolvase marking interfaces important in recombination catalysis and its regulation. Burke, M.E., Arnold, P.H., He, J., Wenwieser, S.V., Rowland, S.J., Boocock, M.R., Stark, W.M. Mol. Microbiol. (2004) [Pubmed]
  30. Structure of NaeI-DNA complex reveals dual-mode DNA recognition and complete dimer rearrangement. Huai, Q., Colandene, J.D., Topal, M.D., Ke, H. Nat. Struct. Biol. (2001) [Pubmed]
  31. The Min DNA inversion enzyme of plasmid p15B of Escherichia coli 15T-: a new member of the Din family of site-specific recombinases. Iida, S., Sandmeier, H., Hübner, P., Hiestand-Nauer, R., Schneitz, K., Arber, W. Mol. Microbiol. (1990) [Pubmed]
  32. The mechanism of recA polA lethality: suppression by RecA-independent recombination repair activated by the lexA(Def) mutation in Escherichia coli. Cao, Y., Kogoma, T. Genetics (1995) [Pubmed]
  33. Alteration of Cre recombinase site specificity by substrate-linked protein evolution. Buchholz, F., Stewart, A.F. Nat. Biotechnol. (2001) [Pubmed]
  34. Interactions of the site-specific recombinases XerC and XerD with the recombination site dif. Blakely, G.W., Sherratt, D.J. Nucleic Acids Res. (1994) [Pubmed]
  35. New approach to cell lineage analysis in mammals using the Cre-loxP system. Sato, M., Yasuoka, Y., Kodama, H., Watanabe, T., Miyazaki, J.I., Kimura, M. Mol. Reprod. Dev. (2000) [Pubmed]
 
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