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Gene Review

int  -  site-specific recombinase

Escherichia coli UTI89

 
 
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Disease relevance of int

  • The argU and DLP12 int genes overlapped at their 3' ends, and argU contained sequence homologous to a portion of the phage P22 attP site [1].
  • This organization of the DLP12 sequences and the presence of the argU/DLP12 int pair in several E. coli strains and closely related species suggest that DLP12 might be an ancestral lambdoid prophage [1].
  • Phage lambdacam112, which contains the chloramphenicol resistance transposon Tn9 and has a deletion of attP and the int gene, will lysogenize Escherichia coli K-12 [2].
  • The vaccinia topoisomerase gene was inducibly expressed in an int-lambda lysogen BL21(DE3) using a T7 RNA polymerase-based transcription system [3].
  • Surprisingly, topoisomerase expression also effected a 200-fold increase in the titer of infectious lambda phage, apparently by promoting int-independent prophage excision [3].
 

High impact information on int

  • The catalytic domain of lambda site-specific recombinase [4].
  • To extend the utility of the reporter gene fusion approach to such studies, we have constructed a gene expression reporter cassette that permits the generation of transcriptional fusions to tnpR encoding resolvase, a site-specific recombinase of the transposable element gamma delta [5].
  • The site-specific recombinase encoded by the yeast plasmid 2-microns circle (FLP) forms a transient covalent linkage with its substrate DNA via a tyrosine residue, which appears to be located near its COOH terminus [6].
  • Cre, the site-specific recombinase from bacteriophage P1, catalyzes a recombination reaction between specific DNA sequences designated as lox sites [7].
  • A block of the lambda genome, int through Q, was not detected in the recombinant molecule [8].
 

Chemical compound and disease context of int

 

Biological context of int

  • Under physiological conditions, integration of lambda DNA into the Escherichia coli chromosome requires the direct participation of only two proteins, the viral int gene product and E. coli integration host factor (IHF) [10].
  • The presence of these genes in recombinant plasmids was detected genetically. lambda int-gene was shown to be expressed in either orientation of insertion in the plasmid [11].
  • Both sib+ and sib- deletions were sequenced, and it was concluded from this and other work that a dyad symmetry present in the b region, 270 base-pairs from int, was necessary for retroregulation [12].
  • The lambda int gene product, integrase, recombines phage and bacterial DNA at a specific site during the integration step of lysogeny [12].
  • Mutational analysis of the lambda int gene: DNA sequence of dominant mutations [13].
 

Anatomical context of int

  • Eleven Salmonella strains were also shown to be invasive in HeLa, int 407, bovine kidney, chick kidney and chick embryonic fibroblast cells [14].
  • In this study, naturally-occurring, monoclonal IgM kappa anti-thymocyte autoantibodies from the neonatal inbred Balb/c mouse-derived hybridoma NMT-1 (NMT-1 mAb), previously reported to identify a restricted CD4+CD8+CD3/lo/int thymocyte subpopulation, have been shown to exhibit extensive polyspecificity [15].
 

Other interactions of int

  • The lambda N protein allows transcription of int from pL [12].
  • One of these regions carries the viral integrase or int function, while the other has previously been suggested to contain the viral RNase H exo activity [16].
 

Analytical, diagnostic and therapeutic context of int

References

  1. Characterization of the cryptic lambdoid prophage DLP12 of Escherichia coli and overlap of the DLP12 integrase gene with the tRNA gene argU. Lindsey, D.F., Mullin, D.A., Walker, J.R. J. Bacteriol. (1989) [Pubmed]
  2. Chromosomal integration of phage lambda by means of a DNA insertion element. MacHattie, L.A., Shapiro, J.A. Proc. Natl. Acad. Sci. U.S.A. (1978) [Pubmed]
  3. Vaccinia DNA topoisomerase I promotes illegitimate recombination in Escherichia coli. Shuman, S. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  4. The catalytic domain of lambda site-specific recombinase. Tirumalai, R.S., Healey, E., Landy, A. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  5. Use of genetic recombination as a reporter of gene expression. Camilli, A., Beattie, D.T., Mekalanos, J.J. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  6. Mutations in the 2-microns circle site-specific recombinase that abolish recombination without affecting substrate recognition. Prasad, P.V., Young, L.J., Jayaram, M. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  7. Isolation and characterization of intermediates in site-specific recombination. Hoess, R., Wierzbicki, A., Abremski, K. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  8. Specialized transduction of colicin E1 DNA in Escherichia coli K-12. Fukumaki, Y., Shimada, K., Takagi, Y. Proc. Natl. Acad. Sci. U.S.A. (1976) [Pubmed]
  9. Site-specific integration of the Streptomyces plasmid pSAM2 in Mycobacterium smegmatis. Martín, C., Mazodier, P., Mediola, M.V., Gicquel, B., Smokvina, T., Thompson, C.J., Davies, J. Mol. Microbiol. (1991) [Pubmed]
  10. Purification and properties of Int-h, a variant protein involved in site-specific recombination of bacteriophage lambda. Lange-Gustafson, B.J., Nash, H.A. J. Biol. Chem. (1984) [Pubmed]
  11. Construction of recombinant plasmid carrying the lambda DNA fragment responsible for prophage integration. Strizhov, N., Tikhomirova, L. Nucleic Acids Res. (1978) [Pubmed]
  12. Deletion analysis of the retroregulatory site for the lambda int gene. Court, D., Huang, T.F., Oppenheim, A.B. J. Mol. Biol. (1983) [Pubmed]
  13. Mutational analysis of the lambda int gene: DNA sequence of dominant mutations. Bear, S.E., Clemens, J.B., Enquist, L.W., Zagursky, R.J. J. Bacteriol. (1987) [Pubmed]
  14. Invasion of Vero cells by Salmonella species. Barrow, P.A., Lovell, M.A. J. Med. Microbiol. (1989) [Pubmed]
  15. Naturally-occurring anti-thymocyte autoantibody which identifies a restricted CD4+CD8+CD3-/lo/int thymocyte subpopulation exhibits extensive polyspecificity. Underwood, J.R., McCall, A., Csar, X.F. Thymus (1996) [Pubmed]
  16. Ribosome-inhibiting proteins, retroviral reverse transcriptases, and RNase H share common structural elements. Ready, M.P., Katzin, B.J., Robertus, J.D. Proteins (1988) [Pubmed]
  17. Identification and characterization of genes involved in excision of the Lactococcus lactis conjugative transposon Tn5276. Rauch, P.J., de Vos, W.M. J. Bacteriol. (1994) [Pubmed]
  18. Directed evolution of the substrate specificities of a site-specific recombinase and an aminoacyl-tRNA synthetase using fluorescence-activated cell sorting (FACS). Santoro, S.W., Schultz, P.G. Methods Mol. Biol. (2003) [Pubmed]
 
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