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Gene Review

traY  -  conjugal transfer protein TraY

Escherichia coli

 
 
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Disease relevance of traY

 

High impact information on traY

  • TraY also binds to the plasmid origin of transfer (oriT), serving as an accessory protein in the nicking of F Factor in preparation for transfer [2].
  • Most TraY mutants had significantly reduced affinity for the TraY oriT binding site while possessing near wild-type stability and nonspecific DNA recognition [2].
  • Biophysical characterization of the TraY protein of Escherichia coli F factor [3].
  • TraY has been classified as a member of the ribbon-helix-helix family of transcription factors but is unusual in appearing to have tandem repeats of the beta alpha alpha motif in the same polypeptide chain [3].
  • However, highly purified TraIp, the traI gene product, nicks oriT in a site- and strand-specific manner in the absence of the traY gene product (TraYp) in vitro (Matson, S.W., and Morton, B.S. (1991) J. Biol. Chem. 266, 16232-16237) [4].
 

Biological context of traY

  • Identification and characterization of the products from the traJ and traY genes of plasmid R100 [5].
  • The first four amino acids at the N-terminal region of the TraJ protein were not essential for positive regulation of expression of traY, the first gene of the traYZ operon [5].
  • The nucleotide sequence of traY shows that this gene may use TTG as the initiation codon and that it encodes a protein of 75 amino acids [5].
  • A series of plasmids related to pOX38-tra715 were constructed which carry either deletion mutations or point mutations in traY [6].
  • In vitro transcription with linear templates could be elicited by altering the traY -10 and -35 hexamers to the consensus sequences [1].
 

Associations of traY with chemical compounds

  • Insertion of a kanamycin-resistance cassette in the traY gene of the pOX38 plasmid, which contains the wild-type PY promoter, resulted in loss of F piliation and transfer ability [6].
  • TraY affinity for variant oriT sequences with base substitutions at or near these guanine bases suggested that two of the three subsites correspond to high-affinity, cooperatively bound imperfect inverted GA(G/T)A repeats [7].
  • Hydroxyl radical footprinting at both oriT and P(Y) sites indicated that bound TraY protected the DNA backbone bordering three adjacent DNA subsites [7].
  • Purified TraY protein had a relative molecular mass of approximately 17,000, as determined by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate [8].
 

Enzymatic interactions of traY

  • Addition of TraYp to nicking reactions catalyzed by helicase I showed no effect on the rate or efficiency of oriT nicking [9].
 

Other interactions of traY

  • These differences presumably define the different alleles of traM and traY previously identified for IncF plasmids by genetic criteria [10].
  • Construction of derivatives of the F plasmid pOX-tra715: characterization of traY and traD mutants that can be complemented in trans [6].
  • Alterations that reduced the effect of template supercoiling on apparent promoter strength in vitro also reduced the effect of the F plasmid TraJ protein on traY expression in vivo [1].
 

Analytical, diagnostic and therapeutic context of traY

  • Analytical ultracentrifugation results for TraY:oligonucleotide complexes were consistent with two of these subsites being bound cooperatively, and the third being occupied at higher TraY concentrations [7].

References

  1. Contributions of promoter context and structure to regulated expression of the F plasmid traY promoter in Escherichia coli K-12. Gaudin, H.M., Silverman, P.M. Mol. Microbiol. (1993) [Pubmed]
  2. Specific DNA recognition by F Factor TraY involves beta-sheet residues. Lum, P.L., Schildbach, J.F. J. Biol. Chem. (1999) [Pubmed]
  3. Biophysical characterization of the TraY protein of Escherichia coli F factor. Schildbach, J.F., Robinson, C.R., Sauer, R.T. J. Biol. Chem. (1998) [Pubmed]
  4. The traY gene product and integration host factor stimulate Escherichia coli DNA helicase I-catalyzed nicking at the F plasmid oriT. Nelson, W.C., Howard, M.T., Sherman, J.A., Matson, S.W. J. Biol. Chem. (1995) [Pubmed]
  5. Identification and characterization of the products from the traJ and traY genes of plasmid R100. Inamoto, S., Yoshioka, Y., Ohtsubo, E. J. Bacteriol. (1988) [Pubmed]
  6. Construction of derivatives of the F plasmid pOX-tra715: characterization of traY and traD mutants that can be complemented in trans. Maneewannakul, K., Kathir, P., Endley, S., Moore, D., Manchak, J., Frost, L., Ippen-Ihler, K. Mol. Microbiol. (1996) [Pubmed]
  7. TraY DNA recognition of its two F factor binding sites. Lum, P.L., Rodgers, M.E., Schildbach, J.F. J. Mol. Biol. (2002) [Pubmed]
  8. Purified Escherichia coli F-factor TraY protein binds oriT. Lahue, E.E., Matson, S.W. J. Bacteriol. (1990) [Pubmed]
  9. Characterization of the Escherichia coli F factor traY gene product and its binding sites. Nelson, W.C., Morton, B.S., Lahue, E.E., Matson, S.W. J. Bacteriol. (1993) [Pubmed]
  10. Origin of transfer of IncF plasmids and nucleotide sequences of the type II oriT, traM, and traY alleles from ColB4-K98 and the type IV traY allele from R100-1. Finlay, B.B., Frost, L.S., Paranchych, W. J. Bacteriol. (1986) [Pubmed]
 
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