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Gene Review

cro  -  Cro

Enterobacteria phage P22

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Disease relevance of cro


High impact information on cro


Chemical compound and disease context of cro

  • The equilibrium stabilities of a complete set of single alanine-substitution mutants of the Arc repressor of bacteriophage P22 have been determined by thermal and urea denaturation experiments [8].

Biological context of cro


Anatomical context of cro


Associations of cro with chemical compounds

  • Purified NH2-terminal fragments, like intact repressor, bind specifically to P22 operator DNA and also mediate positive and negative control of transcription [14].
  • Trp14, the only one tryptophan of Arc repressor monomers, serves as a very sensitive tool for changes of the hydrophobic core of the protein [15].
  • The presence of bioavailable arabinose triggered the production of P22 excisionase and integrase from the reporter plasmid pAraLHB in JL1157, and this led to excision of the cI repressor gene, which is flanked by att sites, and the subsequent irreversible expression of gfp in the original cell and in its progeny [16].
  • The kinetics of its synthesis, as monitored by polyacrylamide gel electrophoresis, is the same as with P22 c+, namely a turn off 8-10 min after infection. - After infection of P22-lysogenic bacteria with either P22 24- k5 or P22 24- k5 c1, much lower amounts of repressor are synthesized but again with the same kinetics [17].

Physical interactions of cro

  • Determination of the nuclear magnetic resonance structure of the DNA-binding domain of the P22 c2 repressor (1 to 76) in solution and comparison with the DNA-binding domain of the 434 repressor [18].

Other interactions of cro


Analytical, diagnostic and therapeutic context of cro


  1. Bacteriophage P22 Cro protein: sequence, purification, and properties. Poteete, A.R., Hehir, K., Sauer, R.T. Biochemistry (1986) [Pubmed]
  2. Primary structure of the phage P22 repressor and its gene c2. Sauer, R.T., Pan, J., Hopper, P., Hehir, K., Brown, J., Poteete, A.R. Biochemistry (1981) [Pubmed]
  3. DNA specificity determinants of Escherichia coli tryptophan repressor binding. Bass, S., Sugiono, P., Arvidson, D.N., Gunsalus, R.P., Youderian, P. Genes Dev. (1987) [Pubmed]
  4. Superinfection exclusion by heteroimmune corynebacteriophages. Groman, N.B., Rabin, M. J. Virol. (1980) [Pubmed]
  5. Changing the DNA-binding specificity of a repressor. Youderian, P., Vershon, A., Bouvier, S., Sauer, R.T., Susskind, M.M. Cell (1983) [Pubmed]
  6. Structure of Arc repressor in solution: evidence for a family of beta-sheet DNA-binding proteins. Breg, J.N., van Opheusden, J.H., Burgering, M.J., Boelens, R., Kaptein, R. Nature (1990) [Pubmed]
  7. Control of gene expression in bacteriophage P22 by a small antisense RNA. I. Characterization in vitro of the Psar promoter and the sar RNA transcript. Liao, S.M., Wu, T.H., Chiang, C.H., Susskind, M.M., McClure, W.R. Genes Dev. (1987) [Pubmed]
  8. Protein stability effects of a complete set of alanine substitutions in Arc repressor. Milla, M.E., Brown, B.M., Sauer, R.T. Nat. Struct. Biol. (1994) [Pubmed]
  9. Scanning mutagenesis of the Arc repressor as a functional probe of operator recognition. Brown, B.M., Milla, M.E., Smith, T.L., Sauer, R.T. Nat. Struct. Biol. (1994) [Pubmed]
  10. Sequence-specific 1H NMR assignment and secondary structure of the Arc repressor of bacteriophage P22, as determined by two-dimensional 1H NMR spectroscopy. Breg, J.N., Boelens, R., George, A.V., Kaptein, R. Biochemistry (1989) [Pubmed]
  11. P22 Arc repressor: transition state properties inferred from mutational effects on the rates of protein unfolding and refolding. Milla, M.E., Brown, B.M., Waldburger, C.D., Sauer, R.T. Biochemistry (1995) [Pubmed]
  12. Solution structure of dimeric Mnt repressor (1-76). Burgering, M.J., Boelens, R., Gilbert, D.E., Breg, J.N., Knight, K.L., Sauer, R.T., Kaptein, R. Biochemistry (1994) [Pubmed]
  13. The bacteriophage 434 operator/repressor system in yeast. Webster, C.I., Brammar, W.J. Microbiology (Reading, Engl.) (1995) [Pubmed]
  14. P22 c2 repressor. Domain structure and function. De Anda, J., Poteete, A.R., Sauer, R.T. J. Biol. Chem. (1983) [Pubmed]
  15. Arc repressor-operator DNA interactions and contribution of Phe10 to binding specificity. Dostál, L., Misselwitz, R., Welfle, H. Biochemistry (2005) [Pubmed]
  16. Site-specific recombination-based genetic system for reporting transient or low-level gene expression. Casavant, N.C., Beattie, G.A., Phillips, G.J., Halverson, L.J. Appl. Environ. Microbiol. (2002) [Pubmed]
  17. Kinetics of c2-repressor synthesis in a regulatory defective P22 mutant. Prell, H.H., Harvey, A.M. Mol. Gen. Genet. (1981) [Pubmed]
  18. Determination of the nuclear magnetic resonance structure of the DNA-binding domain of the P22 c2 repressor (1 to 76) in solution and comparison with the DNA-binding domain of the 434 repressor. Sevilla-Sierra, P., Otting, G., Wüthrich, K. J. Mol. Biol. (1994) [Pubmed]
  19. The bacteriophage P22 arc and mnt repressors. Overproduction, purification, and properties. Vershon, A.K., Youderian, P., Susskind, M.M., Sauer, R.T. J. Biol. Chem. (1985) [Pubmed]
  20. Establishment mode repressor synthesis blunts phage P22 antirepressor activity. Gough, M. J. Mol. Biol. (1977) [Pubmed]
  21. Regulation of gene expression in Salmonella phage P22. II. Regulation of expression of late functions. Prell, H.H. Mol. Gen. Genet. (1975) [Pubmed]
  22. Crystallization of the Arc repressor. Jordan, S.R., Pabo, C.O., Vershon, A.K., Sauer, R.T. J. Mol. Biol. (1985) [Pubmed]
  23. Equilibrium dissociation and unfolding of the Arc repressor dimer. Bowie, J.U., Sauer, R.T. Biochemistry (1989) [Pubmed]
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