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Gene Review

HK022p44  -  cII protein

Enterobacteria phage HK022

 
 
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Disease relevance of HK022p44

  • We have studied the synthesis and stability of cII protein with two experimental systems, phage infection and a cII-producing plasmid [1].
  • When CII protein is provided by a prophage, galactokinase is synthesized at a rate dependent on the concentration of CII protein [2].
 

High impact information on HK022p44

  • The tetrameric cII protein from bacteriophage lambda activates transcription from the phage promoters P(RE), P(I), and P(AQ) by binding to two direct repeats that flank the promoter -35 element [3].
  • Cleavage of the cII protein of phage lambda by purified HflA protease: control of the switch between lysis and lysogeny [4].
  • Six point mutations in the repeated T-T-G-C sequences that flank the -35 consensus region of PRE decreased the apparent affinity of the promoter for cII protein by factors of 4-16 relative to the wild-type affinity [5].
  • Thus low concentrations of guanidine hydrochloride promote a more structured conformation of the CII protein [6].
  • The recombinant CII protein has been purified to homogeneity by ammonium sulfate fractionation followed by two steps of ion-exchange chromatography [7].
 

Biological context of HK022p44

  • There was no apparent difference between the lacI vs. cII target genes of the shuttle vector in either the background or DMN-induced mutant frequencies [8].
  • In the present report, we reveal the molecular nature of the mutations induced by quinoline in the lambda cII gene, which is also a phenotypically selectable marker in the lambda transgene [9].
  • Our previous studies indicated that the impaired lysogenisation of the rpoA341 host is due to a defect in transcriptional activation by the phage CII protein and suggested a role for alphaCTD in this process [10].
 

Associations of HK022p44 with chemical compounds

  • On the other hand, although cyclic AMP is required for efficient lysogeny, it did not appear to influence the synthesis, stability, or activity of cII protein [11].

References

  1. Control of phage lambda development by stability and synthesis of cII protein: role of the viral cIII and host hflA, himA and himD genes. Hoyt, M.A., Knight, D.M., Das, A., Miller, H.I., Echols, H. Cell (1982) [Pubmed]
  2. CII-dependent activation of the pRE promoter of coliphage lambda fused to the Escherichia coli galK gene. Fien, K., Turck, A., Kang, I., Kielty, S., Wulff, D.L., McKenney, K., Rosenberg, M. Gene (1984) [Pubmed]
  3. Crystal structure of bacteriophage lambda cII and its DNA complex. Jain, D., Kim, Y., Maxwell, K.L., Beasley, S., Zhang, R., Gussin, G.N., Edwards, A.M., Darst, S.A. Mol. Cell (2005) [Pubmed]
  4. Cleavage of the cII protein of phage lambda by purified HflA protease: control of the switch between lysis and lysogeny. Cheng, H.H., Muhlrad, P.J., Hoyt, M.A., Echols, H. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  5. Kinetic analysis of mutations affecting the cII activation site at the PRE promoter of bacteriophage lambda. Shih, M.C., Gussin, G.N. Proc. Natl. Acad. Sci. U.S.A. (1984) [Pubmed]
  6. Disorder-order transition of lambda CII promoted by low concentrations of guanidine hydrochloride suggests a stable core and a flexible C-terminus. Datta, A.B., Roy, S., Parrack, P. Eur. J. Biochem. (2003) [Pubmed]
  7. Purification and crystallization of CII: an unstable transcription activator from phage lambda. Datta, A.B., Chakrabarti, P., Subramanya, H.S., Parrack, P. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  8. Hepatic lacI and cII mutation in transgenic (lambdaLIZ) rats treated with dimethylnitrosamine. Gollapudi, B.B., Jackson, K.M., Stott, W.T. Mutat. Res. (1998) [Pubmed]
  9. Hepatocarcinogen quinoline induces G:C to C:G transversions in the cII gene in the liver of lambda/lacZ transgenic mice (MutaMouse). Suzuki, T., Wang, X., Miyata, Y., Saeki, K., Kohara, A., Kawazoe, Y., Hayashi, M., Sofuni, T. Mutat. Res. (2000) [Pubmed]
  10. The Escherichia coli RNA polymerase alpha subunit and transcriptional activation by bacteriophage lambda CII protein. Gabig, M., Obuchowski, M., Ciesielska, A., Latała, B., Wegrzyn, A., Thomas, M.S., Wegrzyn, G. Acta Biochim. Pol. (1998) [Pubmed]
  11. Control of bacteriophage lambda CII activity by bacteriophage and host functions. Rattray, A., Altuvia, S., Mahajna, G., Oppenheim, A.B., Gottesman, M. J. Bacteriol. (1984) [Pubmed]
 
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