Disease relevance of tetR

• TetR repressor proteins from the Agrobacterium tet system and from RP4 interacted with the heterologous operators [1].
• The fates of the chromosome ori and ter loci were monitored by visualization by using derivatives of LacI and TetR fused to fluorescent proteins in E. coli strains that carry operator arrays at the appropriate locations [2].
• We used E. coli strains with either TetR or the reverse variant revTetR(r2), while only TetR was employed in Salmonella [3].

High impact information on tetR

• There is, in addition, significant amino acid sequence homology between an NH2-terminal region of the Tn10 TetR repressor and the DNA recognition regions of other DNA-binding proteins [4].
• Two open reading frames of divergent polarity have been assigned to a regulatory gene (tetR) and a gene encoding a resistance protein (tetA) [5].
• Tigecycline induced the Tet(B) protein approximately four times more efficiently than tetracycline, as determined by Western blotting, indicating that it is at least recognized by a TetR repressor [6].
• Expression of beta-galactosidase by the fusion plasmid pUB3610 remained subject to regulatory control by the TetR repressor protein, with the presence of tetracyclines in the growth medium leading to a 12-fold induction of beta-galactosidase synthesis [7].
• It randomly fuses the TetR-inducing peptide Tip to the affected reading frame [8].

Biological context of tetR

• It contains three 38-bp inverted repeats, and (in this order) a new orfI, a resolution site (res), genes encoding resolvase (tnpR), transposase (tnpA), tetracycline-resistance (TcR) repressor (tetR), TcR (tetA) and a truncated transposase gene (tnpA') [9].
• There is 47% amino acid sequence homology between the deduced sequences of the Tn10 and RP1/Tn1721 TetR proteins [4].
• Contrary to dimeric TetR, scTetR allows the construction of scTetR mutants, in which one subunit contains a defective inducer binding site while the other is functional [10].
• Random insertion of a TetR-inducing peptide tag into Escherichia coli proteins allows analysis of protein levels by induction of reporter gene expression [8].

References