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Gene Review

cro  -  Cro protein

Escherichia coli UTI89

 
 
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Disease relevance of cro

 

High impact information on cro

  • This reaction required, in addition to pol V, UmuD', RecA, and single-stranded DNA (ssDNA)-binding protein. pol V produced point mutations at a frequency of 2.1 x 10(-4) per nucleotide (2.1% per cro gene), 41-fold higher than DNA polymerase III holoenzyme [4].
  • This was done by in vitro UV irradiation and deamination of a plasmid carrying the cro gene, followed by photoreactivation, and assaying uracils in DNA by their ability to cause Cro- mutations in an indicator strain that was deficient in uracil DNA N-glycosylase [5].
  • We show that cytidine, as a free nucleoside, inhibits the binding of rho to lambda cro mRNA and is a competitive inhibitor of rho-ATPase activity with lambda cro mRNA as cofactor [6].
  • This shift may be induced by a bend in the OR3 operator DNA at the GC 9 base pair to accommodate the operator for the binding of the Cro protein dimer [3].
  • The 434 cro protein as deduced from the DNA sequence is a highly basic protein of 71 amino acid residues with a calculated molecular weight of 8089 [7].
 

Biological context of cro

  • However, T16A Rho was less efficient in terminating transcription than was wt Rho and had a lowered kcat for ATP hydrolysis with cro RNA as co-factor [8].
  • As expected, no analogies with (dimeric) repressors and cro proteins which have the characteristic helix-turn-helix motif have been observed [9].
 

Anatomical context of cro

 

Associations of cro with chemical compounds

  • Exposed tyrosine residues of lambda cro repressor protein evidenced by nitration and photo CIDNP experiments [11].
 

Analytical, diagnostic and therapeutic context of cro

References

  1. Biochemical analysis of UV mutagenesis in Escherichia coli by using a cell-free reaction coupled to a bioassay: identification of a DNA repair-dependent, replication-independent pathway. Cohen-Fix, O., Livneh, Z. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  2. Purification and characterization of the Ner repressor of bacteriophage Mu. Kukolj, G., Tolias, P.P., DuBow, M.S. FEBS Lett. (1989) [Pubmed]
  3. 1H NMR study of the interaction of bacteriophage lambda Cro protein with the OR3 operator. Evidence for a change of the conformation of the OR3 operator on binding. Kirpichnikov, M.P., Hahn, K.D., Buck, F., Rüterjans, H., Chernov, B.K., Kurochkin, A.V., Skryabin, K.G., Bayev, A.A. Nucleic Acids Res. (1984) [Pubmed]
  4. Highly mutagenic replication by DNA polymerase V (UmuC) provides a mechanistic basis for SOS untargeted mutagenesis. Maor-Shoshani, A., Reuven, N.B., Tomer, G., Livneh, Z. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  5. Deamination of cytosine-containing pyrimidine photodimers in UV-irradiated DNA. Significance for UV light mutagenesis. Barak, Y., Cohen-Fix, O., Livneh, Z. J. Biol. Chem. (1995) [Pubmed]
  6. Cytosine nucleoside inhibition of the ATPase of Escherichia coli termination factor rho: evidence for a base specific interaction between rho and RNA. Richardson, L.V., Richardson, J.P. Nucleic Acids Res. (1992) [Pubmed]
  7. Nucleotide sequence of the cro-cII-oop region of bacteriophage 434 DNA. Grosschedl, R., Schwarz, E. Nucleic Acids Res. (1979) [Pubmed]
  8. A vector for controlled, high-yield production of specifically mutated proteins in Escherichia coli: test of a putative cytidine-binding domain in Rho factor and its Thr16----Ala mutant. Richardson, L.V., Richardson, J.P. Gene (1992) [Pubmed]
  9. The GATATC-modification enzyme EcoRV is closely related to the GATC-recognizing methyltransferases DpnII and dam from E. coli and phage T4. Lauster, R., Kriebardis, A., Guschlbauer, W. FEBS Lett. (1987) [Pubmed]
  10. mRNA containing an extended Shine-Dalgarno sequence is translated independently of ribosomal protein S1. Balakin, A.G., Bogdanova, S.L., Skripkin, E.A. Biochem. Int. (1992) [Pubmed]
  11. Exposed tyrosine residues of lambda cro repressor protein evidenced by nitration and photo CIDNP experiments. Shirakawa, M., Kawata, Y., Lee, S.J., Akutsu, H., Sakiyama, F., Kyogoku, Y. J. Biochem. (1985) [Pubmed]
  12. Studies of the structure of bacteriophage lambda cro protein in solution. Analysis of the circular dichroism data. Bolotina, I.A., Kurochkin, A.V., Kirpichnikov, M.P. FEBS Lett. (1983) [Pubmed]
 
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