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Article

The role of the N terminus in Tet repressor for tet operator binding determined by a mutational analysis.

The Journal of biological chemistry - 25 Jan 1992

Berens C, Altschmied L, Hillen W

Abstract excerpt

The N-terminal residues preceding the alpha-helix-turn-alpha-helix motif on the Tn10 Tet repressor protein were probed by oligonucleotide-directed deletion mutagenesis for their role in protein activity. All deletion mutants showed decreased repression in vivo, emphasizing the importance of the N terminus for tet operator binding. Only two of the mutants, TetR delta 2-23 and TetR delta 3-8 displayed a reduced...

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PMID: 1309804

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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The role of the N terminus in Tet repressor for tet operator binding determined by a mutational analysis.PMID 1309804Read ↗

Amino acids determining operator binding specificity in the helix-turn-helix motif of Tn10 Tet repressor.Semantic proximity Read ↗

Noninducible Tet repressor mutations map from the operator binding motif to the C terminus.Semantic proximity Read ↗

Quantitative analysis of Tn10 Tet repressor binding to a complete set of tet operator mutants.Semantic proximity Read ↗

Stepwise selection of TetR variants recognizing tet operator 6C with high affinity and specificity.Semantic proximity Read ↗

Mechanism of Tet repressor induction by tetracyclines: length compensates for sequence in the alpha8-alpha9 loop.Semantic proximity Read ↗

Proximity probing of Tet repressor to tet operator by dimethylsulfate reveals protected and accessible functions for each recognized base-pair in the major groove.Semantic proximity Read ↗

A peptide triggers allostery in tet repressor by binding to a unique site.Semantic proximity Read ↗

Conformational changes necessary for gene regulation by Tet repressor assayed by reversible disulfide bond formation.Semantic proximity Read ↗

Stepwise selection of TetR variants recognizing tet operator 4C with high affinity and specificity.Semantic proximity Read ↗

Structural investigation of Tet repressor loop 154-167: a time-resolved fluorescence study of three single Trp mutants.Semantic proximity Read ↗

Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance.Semantic proximity Read ↗

Conformational changes induced in the Tet repressor protein TetR(B) upon operator or anhydrotetracycline binding as revealed by time-resolved fluorescence spectroscopy on single tryptophan mutants.Semantic proximity Read ↗

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