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Gene Review

HK97p41  -  Gp51

Enterobacteria phage HK97

Synonyms: 51, cro
 
 
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Disease relevance of HK97p41

  • The Cro protein from bacteriophage lambda has a dimeric alpha+beta fold that evolved from an ancestral all-alpha monomer [1].
  • The alternating pyrimidine-purine elements CA, CAC, and CACA are anisotropically flexible, as deduced from gel circularization assays on point mutations and single-base mismatches in the OR3 site of lambda phage alone and in the specific complex with the Cro protein [2].
 

High impact information on HK97p41

  • Here we use analysis of sequence alignments to show that Ala-33, a small side chain in the hydrophobic "ball-and-socket" dimer interface of lambda Cro, was a much larger tryptophan side chain at a previous point in evolution [1].
  • Hydroxyl radical "footprinting": high-resolution information about DNA-protein contacts and application to lambda repressor and Cro protein [3].
  • The comparison of binding strengths and the conformation of Cro repressor in the two protein-DNA complexes shows that base pair differences between the two halves of the OR3 operator affect the binding of Cro repressor protein [4].
  • lambda Cro repressor protein is titrated with two half-operator DNA duplexes comprising the right and left halves of the major binding site on phage lambda DNA, the OR3 operator [4].
  • The intersubunit connection includes a region within the protein core that is structurally reminiscent of the "ball and socket" motif seen in the immunoglobulins and T-cell receptors.The crystal structure of the Cro complex is consistent with virtually all available biochemical and related data [5].
 

Chemical compound and disease context of HK97p41

 

Biological context of HK97p41

  • Folding kinetics of phage 434 Cro protein [8].
  • The thermal unfolding of the wild-type Cro repressor, its disulfide-bridged mutant Cro-V55C (with the Val-55 --> Cys single amino acid substitution), and a CNBr-fragment (13-66)2 of Cro-V55C was studied by Fourier transform infrared spectroscopy and dynamic light scattering [9].
  • It is unlikely that repression of PFR by CI or Cro binding to OFR can account in full for the antivirulence phenotype conferred by this element, since PFR is such a weak promoter [10].
  • While the residues in the HTH motif in 434 Cro have relatively larger positive correlation coefficients of motions with other residues within the HTH motif, such correlations are not large in the HTH motif of 434 repressor [11].
  • From a series of amino acid sequence and gene sequence comparisons, it appears that a number of other DNA-binding proteins have an alpha-helical DNA-binding region similar to that seen in Cro [12].
 

Anatomical context of HK97p41

  • The interaction of the cro protein with the non-operator DNAs, calf thymus DNA and a synthetic 10 bp duplex, reveals no visible CD changes at all [13].
 

Associations of HK97p41 with chemical compounds

  • 434 Cro folding under NMR solution conditions is two-state as indicated by coincident urea denaturation curves from circular dichroism and intrinsic fluorescence measurements [14].
  • In contrast to lambda(6-85), sharp and distinct aromatic (1)H NMR signals without exchange broadening characterize the native and urea-denatured 434 Cro forms at equilibrium at 20 degrees C, indicating slow interconversion on the NMR time scale [8].
  • Moreover, the aspartic acid in the mutant was found to form a capping interaction with the amino terminus of the third alpha-helix of Cro [15].
  • Helix formation is observed for the 434 Cro helix 1 and helix 2 peptides in water, for all the peptides in 40% TFE and for none in 7 M urea [16].
 

Other interactions of HK97p41

  • Cro protein recognizes 4 base pairs in a lambda operator half-site in different ways than cI repressor [17].
 

Analytical, diagnostic and therapeutic context of HK97p41

  • Analytical ultracentrifugation experiments confirm that 434 Cro is monomeric even at the high NMR concentrations [14].

References

  1. Retroevolution of lambda Cro toward a stable monomer. LeFevre, K.R., Cordes, M.H. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  2. CA runs increase DNA flexibility in the complex of lambda Cro protein with the OR3 site. Lyubchenko, Y.L., Shlyakhtenko, L.S., Appella, E., Harrington, R.E. Biochemistry (1993) [Pubmed]
  3. Hydroxyl radical "footprinting": high-resolution information about DNA-protein contacts and application to lambda repressor and Cro protein. Tullius, T.D., Dombroski, B.A. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  4. Different interactions of Cro repressor dimer with the left and right halves of OR3 operator DNA. Baleja, J.D., Anderson, W.F., Sykes, B.D. J. Biol. Chem. (1991) [Pubmed]
  5. Crystal structure of lambda-Cro bound to a consensus operator at 3.0 A resolution. Albright, R.A., Matthews, B.W. J. Mol. Biol. (1998) [Pubmed]
  6. Thermodynamic analysis of the structural stability of phage 434 Cro protein. Padmanabhan, S., Laurents, D.V., Fernández, A.M., Elias-Arnanz, M., Ruiz-Sanz, J., Mateo, P.L., Rico, M., Filimonov, V.V. Biochemistry (1999) [Pubmed]
  7. Intersubunit disulfide-bonded lambda-Cro protein. Shirakawa, M., Matsuo, H., Kyogoku, Y. Protein Eng. (1991) [Pubmed]
  8. Folding kinetics of phage 434 Cro protein. Laurents, D.V., Corrales, S., Elías-Arnanz, M., Sevilla, P., Rico, M., Padmanabhan, S. Biochemistry (2000) [Pubmed]
  9. Secondary structure and oligomerization behavior of equilibrium unfolding intermediates of the lambda cro repressor. Fabian, H., Fälber, K., Gast, K., Reinstädler, D., Rogov, V.V., Naumann, D., Zamyatkin, D.F., Filimonov, V.V. Biochemistry (1999) [Pubmed]
  10. A novel antivirulence element in the temperate bacteriophage HK022. Carlson, N.G., Little, J.W. J. Bacteriol. (1993) [Pubmed]
  11. A comparative study of dynamic structures between phage 434 Cro and repressor proteins by normal mode analysis. Wako, H., Tachikawa, M., Ogawa, A. Proteins (1996) [Pubmed]
  12. High resolution structural studies of Cro repressor protein and implications for DNA recognition. Ohlendorf, D.H., Anderson, W.F., Takeda, Y., Matthews, B.W. J. Biomol. Struct. Dyn. (1983) [Pubmed]
  13. The absence of non-local conformational changes in OR3 operator DNA on complexing with the cro repressor. Kirpichnikov, M.P., Yartzev, A.P., Minchenkova, L.E., Chernov, B.K., Ivanov, V.I. J. Biomol. Struct. Dyn. (1985) [Pubmed]
  14. Three-dimensional solution structure and stability of phage 434 Cro protein. Padmanabhan, S., Jiménez, M.A., Gonzalez, C., Sanz, J.M., Giménez-Gallego, G., Rico, M. Biochemistry (1997) [Pubmed]
  15. Helix-capping interaction in lambda Cro protein: a free energy simulation analysis. Tidor, B. Proteins (1994) [Pubmed]
  16. Folding propensities of synthetic peptide fragments covering the entire sequence of phage 434 Cro protein. Padmanabhan, S., Jiménez, M.A., Rico, M. Protein Sci. (1999) [Pubmed]
  17. Phage lambda Cro protein and cI repressor use two different patterns of specific protein-DNA interactions to achieve sequence specificity in vivo. Benson, N., Youderian, P. Genetics (1989) [Pubmed]
 
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