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Gene Review:

ECs1353 - protein TerB

Escherichia coli O157:H7 str. Sakai

Gottlieb, P.A. et al., Duggan, L.J. et al., Andersen, P.A. et al., Bierne, H. et al., Duggan, L.J. et al., et al.

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Disease relevance of ECs1353

A new B. subtilis-E. coli shuttle plasmid was designed to allow the insertion of either the Terl (B. subtilis) or TerB (E. coli) terminator at the same site and in the active orientation in relation to the approaching replication fork generated in either organism [1].

High impact information on ECs1353

For uracil substitutions, potential hydrophobic sites were identified at six positions in the TerB DNA [2].
Each of four consensus guanine residues in the TerB-binding site was replaced by 7-deazaguanine, 2-aminopurine, or inosine nucleobase analogues, and each thymine by a uracil analogue [2].
Extensive contacts between the Tus protein and the TerB sequence were observed in the highly conserved 11 base-pair "core" sequence common to all identified Ter sites [3].
The measured equilibrium binding constant (KD) for the chromosomal TerB site in KG buffer (50 mM Tris-Cl, 150 mM potassium glutamate, 25 degrees C, pH 7.5, 0.1 mM dithiothreitol, 0.1 mM EDTA, and 100 micrograms/ml bovine serum albumin) was 3.4 x 10(-13) M [3].
The distribution of contacts along the TerB sequence was consistent with the functional polarity of the Tus-Ter complex and suggested possible mechanisms for the impediment of protein translocation along DNA [3].

Biological context of ECs1353

The Escherichia coli replication terminator protein (Tus) binds tightly and specifically to termination sites such as TerB in order to halt DNA replication [4].
We found that flanking sequences do affect replication arrest efficiency, a weak arrest being correlated with the presence of an AT-rich region which is replicated just before TerB [5].

Associations of ECs1353 with chemical compounds

Using the substitution of bromodeoxyuridine at position 8 in the TerB DNA, Tus protein was covalently attached to the DNA, and by trypsin digestion a fragment of Tus was isolated [6].

References

Functional specificity of the replication fork-arrest complexes of Bacillus subtilis and Escherichia coli: significant specificity for Tus-Ter functioning in E. coli. Andersen, P.A., Griffiths, A.A., Duggin, I.G., Wake, R.G. Mol. Microbiol. (2000) [Pubmed]
Using modified nucleotides to map the DNA determinants of the Tus-TerB complex, the protein-DNA interaction associated with termination of replication in Escherichia coli. Duggan, L.J., Hill, T.M., Wu, S., Garrison, K., Zhang, X., Gottlieb, P.A. J. Biol. Chem. (1995) [Pubmed]
Equilibrium, kinetic, and footprinting studies of the Tus-Ter protein-DNA interaction. Gottlieb, P.A., Wu, S., Zhang, X., Tecklenburg, M., Kuempel, P., Hill, T.M. J. Biol. Chem. (1992) [Pubmed]
Interaction of the Escherichia coli replication terminator protein (Tus) with DNA: a model derived from DNA-binding studies of mutant proteins by surface plasmon resonance. Neylon, C., Brown, S.E., Kralicek, A.V., Miles, C.S., Love, C.A., Dixon, N.E. Biochemistry (2000) [Pubmed]
Flanking sequences affect replication arrest at the Escherichia coli terminator TerB in vivo. Bierne, H., Ehrlich, S.D., Michel, B. J. Bacteriol. (1994) [Pubmed]
Identification of a Tus protein segment that photo-cross-links with TerB DNA and elucidation of the role of certain thymine methyl groups in the Tus-TerB complex using halogenated uracil analogues. Duggan, L.J., Asmann, P.T., Hill, T.M., Gottlieb, P.A. Biochemistry (1996) [Pubmed]

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