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Gene Review

int  -  Gp30

Enterobacteria phage HK97

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Disease relevance of int

  • However, if ORF2 does represent an xis gene, then this putative integration module would possess a notable difference from that of other temperate phages in the inversion of the positions of int and xis relative to attP [1].
  • Characterization of the cryptic lambdoid prophage DLP12 of Escherichia coli and overlap of the DLP12 integrase gene with the tRNA gene argU [2].
  • Expression of vaccinia virus DNA topoisomerase I in a lambda lysogen of Escherichia coli promotes int-independent excisive recombination of the prophage [3].
  • The blocked-migration model predicts frequent genetic exchange in the int xis region near the attachment site if Int-mediated recombination occurs between lambda phage with homologous attachment sites [4].
  • Sequence analysis revealed that the integrase of the Bacteroides conjugative transposon CTnDOT (IntDOT) might be a member of the tyrosine recombinase family because IntDOT has five of six highly conserved residues found in the catalytic domains of tyrosine recombinases [5].

High impact information on int

  • A TYB-encoded protein, p90-TYB, contains amino acid sequences that are similar to those of retroviral integrase proteins [6].
  • They are, moreover, defective for the growth of bacteriophage Mu, for precise excision of transposable antibiotic resistance determinants and for the synthesis of the lambda int gene product [7].
  • With the assistance of accessory proteins that induce DNA loops, Int bridges pairs of distinct arm- and core-type DNA binding sites to form synapsed recombination complexes, which then recombine via a Holliday junction (HJ) intermediate [8].
  • These structures accommodate simultaneous binding of Int to direct-repeat arm sites and indirect-repeat core sites and afford a new view of the higher-order recombinogenic complexes [8].
  • Integrase-mediated DNA cleavage before or immediately after synapsis is required to stabilize the synaptic assemblies [9].

Chemical compound and disease context of int

  • Lambda's int gene contains an anomalously high frequency of the rare arginine codons AGA and AGG when compared to genes of Escherichia coli or to the rest of phage lambda [10].
  • Holliday junctions (HJ) are the central intermediates in both homologous recombination and site-specific recombination performed by tyrosine recombinases such as the bacteriophage lambda Integrase (Int) protein [11].

Biological context of int


Anatomical context of int

  • This indicates that depletion of the rare Arg tRNA due to ribosome stalling at multiple AGA and AGG codons on the overexpressed int mRNA underlies all of these phenomena [14].
  • We also demonstrate that scIHF2 is stably expressed in HeLa cells, that it is localized primarily in the cell nucleus and that it triggers integrative recombination in mammalian cells by wild-type integrase [15].

Associations of int with chemical compounds

  • In this study, we show that expression of the natural int gene may also be modulated by rare arginine codon usage, and we explore this mechanism [10].
  • Temperature-stable chloramphenicol resistance (CmR at 40 degrees C) conferred by low-multiplicity infection with lambda::Tn9 cI857 lysates (Tn9 sites tested: 22.60 or 24.08 kb, in the b region, or 28.41 kb, in int) is usually due to a lambda::Tn9 plasmid (p lambda CM) formed by a deletion penetrating the lambda immunity region [16].
  • Synthesis or stability of int and ampicillin resistance mRNAs is not affected, although a portion of the untranslated int mRNA appears to be modified in a site-specific fashion [14].
  • From this we have cloned and characterized a 188-amino acid, protease-resistant, carboxy-terminal fragment (C170) that we believe is the minimal catalytically competent domain of Int. C170 has topoisomerase activity and converts att suicide substrates to the covalent phosphotyrosine complexes characteristic of recombination intermediates [17].
  • Int is a tyrosine recombinase that binds to DNA core sites via a C-terminal catalytic domain and to a collection of arm DNA sites, distant from the site of recombination, via its N-terminal domain [18].

Analytical, diagnostic and therapeutic context of int

  • The ligation product is then transformed into a strain that contains the int-carrying plasmid [19].
  • Complementation tests demonstrated that the deletions in all three strains removed both att P and the int gene, i,e., DNA from both prophage ends [20].
  • A gel mobility shift assay has been used to show that, in the absence of accessory proteins, Int can align and hold together two DNA molecules, each with an attachment site, to form stable non-covalent 'bimolecular complexes'. Each attachment site must have both core and arm binding sites for Int to participate in a bimolecular complex [21].
  • NMR titration data with a peptide corresponding to Xis residues 57-69 strongly suggest that the carboxyl-terminal tail of Xis and the alpha-helix of the aminoterminal domain of Int comprise the primary interaction surface for these two proteins [22].
  • The phages were characterized by restriction enzyme analysis, hybridization with probes for toxin genes and selected phage DNA such as the P gene, integrase gene and IS1203, and by PCR studies and partial sequencing of selected DNA regions in the integrase to stx(2) region of the phages [23].


  1. Cloning and DNA sequence analysis of the region containing attP of the temperate phage phi AR29 of Prevotella ruminicola AR29. Gregg, K., Kennedy, B.G., Klieve, A.V. Microbiology (Reading, Engl.) (1994) [Pubmed]
  2. 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]
  3. Recombination mediated by vaccinia virus DNA topoisomerase I in Escherichia coli is sequence specific. Shuman, S. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  4. Some properties of site-specific and general recombination inferred from int-initiated exchanges by bacteriophage lambda. Echols, H., Green, L. Genetics (1979) [Pubmed]
  5. Characterization of a conjugative transposon integrase, IntDOT. Malanowska, K., Salyers, A.A., Gardner, J.F. Mol. Microbiol. (2006) [Pubmed]
  6. The DNA intermediate in yeast Ty1 element transposition copurifies with virus-like particles: cell-free Ty1 transposition. Eichinger, D.J., Boeke, J.D. Cell (1988) [Pubmed]
  7. Direct role of the himA gene product in phage lambda integration. Miller, H.I., Nash, H.A. Nature (1981) [Pubmed]
  8. Arm sequences contribute to the architecture and catalytic function of a lambda integrase-Holliday junction complex. Radman-Livaja, M., Shaw, C., Azaro, M., Biswas, T., Ellenberger, T., Landy, A. Mol. Cell (2003) [Pubmed]
  9. Viewing single lambda site-specific recombination events from start to finish. Mumm, J.P., Landy, A., Gelles, J. EMBO J. (2006) [Pubmed]
  10. Modulation of lambda integrase synthesis by rare arginine tRNA. Zahn, K., Landy, A. Mol. Microbiol. (1996) [Pubmed]
  11. Holliday junction-binding peptides inhibit distinct junction-processing enzymes. Kepple, K.V., Boldt, J.L., Segall, A.M. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  12. Generation of single base-pair deletions, insertions, and substitutions by a site-specific recombination system. Leong, J.M., Nunes-Düby, S.E., Landy, A. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  13. Site-specific DNA condensation and pairing mediated by the int protein of bacteriophage lambda. Better, M., Lu, C., Williams, R.C., Echols, H. Proc. Natl. Acad. Sci. U.S.A. (1982) [Pubmed]
  14. Overexpression of an mRNA dependent on rare codons inhibits protein synthesis and cell growth. Zahn, K. J. Bacteriol. (1996) [Pubmed]
  15. Activation of site-specific DNA integration in human cells by a single chain integration host factor. Corona, T., Bao, Q., Christ, N., Schwartz, T., Li, J., Dröge, P. Nucleic Acids Res. (2003) [Pubmed]
  16. Endpoint distribution for deletions into imm lambda region forming p lambda CM replicons: phage lambda gene rex affects plasmid establishment. MacHattie, L.A. Gene (1985) [Pubmed]
  17. The catalytic domain of lambda site-specific recombinase. Tirumalai, R.S., Healey, E., Landy, A. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  18. DNA arms do the legwork to ensure the directionality of lambda site-specific recombination. Radman-Livaja, M., Biswas, T., Ellenberger, T., Landy, A., Aihara, H. Curr. Opin. Struct. Biol. (2006) [Pubmed]
  19. A versatile method for integration of genes and gene fusions into the lambda attachment site of Escherichia coli. Atlung, T., Nielsen, A., Rasmussen, L.J., Nellemann, L.J., Holm, F. Gene (1991) [Pubmed]
  20. Isolation and characterization of plaque-forming lambdadnaZ+ transducing bacteriophages. Walker, J.R., Henson, J.M., Lee, C.S. J. Bacteriol. (1977) [Pubmed]
  21. Synaptic intermediates in bacteriophage lambda site-specific recombination: integrase can align pairs of attachment sites. Segall, A.M., Nash, H.A. EMBO J. (1993) [Pubmed]
  22. Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. Warren, D., Sam, M.D., Manley, K., Sarkar, D., Lee, S.Y., Abbani, M., Wojciak, J.M., Clubb, R.T., Landy, A. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  23. Mosaic structure of Shiga-toxin-2-encoding phages isolated from Escherichia coli O157:H7 indicates frequent gene exchange between lambdoid phage genomes. Johansen, B.K., Wasteson, Y., Granum, P.E., Brynestad, S. Microbiology (Reading, Engl.) (2001) [Pubmed]
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