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Gene Review

int  -  hypothetical protein

Escherichia coli

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Disease relevance of int

  • The lambda int gene product, integrase, recombines phage and bacterial DNA at a specific site during the integration step of lysogeny [1].
  • Retroregulation of int is caused, in part, by processing of the pL transcript at the sib site by RNase III of Escherichia coli [1].
  • The lambda phage att site: functional limits and interaction with Int protein [2].
  • If the level of Int protein synthesis is high enough, the prophage excision can be observed in the absence of Xis product [3].
  • Integration of bacteriophage Mx8 into the Myxococcus xanthus chromosome causes a structural alteration at the C-terminal region of the IntP protein [4].

High impact information on int

  • The rate of synthesis of cl and Int after infection by lambda is severely reduced in a strain carrying a himA gene deletion [5].
  • The minimal phage att site is composed of approximately 240-base pairs and four distinct binding sites for Int protein, at least three of which are crucial for function [2].
  • DNase I protection experiments showed that MBP-INT proteins containing the C-terminal end of Int bound to the ends of the transposon and adjacent plasmid DNA [6].
  • Different proteins, consisting of fragments of Tn916 Int protein fused to the C-terminal end of maltose binding protein (MBP) were purified from Escherichia coli [6].
  • The increase of Int protein synthesis also takes place when the rare arginine codons AGA and AGG at positions 3 and 4 are changed to common arginine CGT or lysine AAA codons but not to rare isoleucine ATA codons [7].

Chemical compound and disease context of int

  • We concluded that Int protein of phage 16-3 belongs to the integrase family of tyrosine recombinases [8].

Biological context of int

  • 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 [1].
  • Therefore, cell growth and Int synthesis inhibition may be due to ribosome stalling and premature release of peptidyl-tRNAArg4 from the ribosome at the rare arginine codons of the first tandem, which leads to cell starvation for the specific tRNA [7].
  • The Int protein had an apparent molecular mass of 42.0 kDa, corresponding well with that (45.5 kDa) predicted from the DNA sequence [9].
  • These results are indicative of site-specific interaction of Int with the attP site, the reaction prerequisite for integration and excision of the phi g1e genome into and/or out of the host chromosome [9].
  • The Int proteins of bacteriophages HK022 and lambda promote recombination between phage and bacterial attachment sites [10].

Associations of int with chemical compounds

  • Amino-acid sequencing revealed that the N-terminal 20 amino-acids of the purified Int protein completely coincided with those deduced from the DNA sequence, although deficient in the first methionine [9].

Analytical, diagnostic and therapeutic context of int


  1. Deletion analysis of the retroregulatory site for the lambda int gene. Court, D., Huang, T.F., Oppenheim, A.B. J. Mol. Biol. (1983) [Pubmed]
  2. The lambda phage att site: functional limits and interaction with Int protein. Hsu, P.L., Ross, W., Landy, A. Nature (1980) [Pubmed]
  3. Functional analysis of hybrid plasmids carrying genes for lambda site-specific recombination. Strizhov, N., Soukovatitsin, V., Ksenzenko, V., Tikhomirova, L., Bayev, A. Gene (1980) [Pubmed]
  4. Integration of bacteriophage Mx8 into the Myxococcus xanthus chromosome causes a structural alteration at the C-terminal region of the IntP protein. Tojo, N., Sanmiya, K., Sugawara, H., Inouye, S., Komano, T. J. Bacteriol. (1996) [Pubmed]
  5. Multilevel regulation of bacteriophage lambda lysogeny by the E. coli himA gene. Miller, H.I. Cell (1981) [Pubmed]
  6. Conjugative transposition: Tn916 integrase contains two independent DNA binding domains that recognize different DNA sequences. Lu, F., Churchward, G. EMBO J. (1994) [Pubmed]
  7. The pair of arginine codons AGA AGG close to the initiation codon of the lambda int gene inhibits cell growth and protein synthesis by accumulating peptidyl-tRNAArg4. Olivares-Trejo, J.J., Bueno-Martínez, J.G., Guarneros, G., Hernández-Sánchez, J. Mol. Microbiol. (2003) [Pubmed]
  8. Identification of site-specific recombination genes int and xis of the Rhizobium temperate phage 16-3. Semsey, S., Papp, I., Buzas, Z., Patthy, A., Orosz, L., Papp, P.P. J. Bacteriol. (1999) [Pubmed]
  9. Purification and DNA-binding properties of the integrase protein Int encoded by Lactobacillus plantarum phage. Yasukawa, H., Kakikawa, M., Masamune, Y., Taketo, A., Kodaira, K.I. Gene (1997) [Pubmed]
  10. Specificity determinants in the attachment sites of bacteriophages HK022 and lambda. Nagaraja, R., Weisberg, R.A. J. Bacteriol. (1990) [Pubmed]
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