Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Intragenic complementation between Escherichia coli trp repressors with different defects in the tryptophan-binding pocket.

Gene - 1 Aug 1992

Storbakk N, Oxender D L, el-Gewely M R

Abstract excerpt

Site-directed mutagenesis of the trpR gene (encoding the trp repressor, TrpR) was used to replace Gly85 with tryptophan (Trp or W), in order to place Trp near its normal location in the L-tryptophan(L-W)-binding pocket. The resulting mutant protein (G85W) exhibits weak, but significant repressor activity in vivo that is independent of the presence of L-W in the media. This mutant negatively complements the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Alleles
Share to Bacterial Proteins
Share to Base Sequence

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Binding Sites

Share to DNA, Bacterial

Share to Escherichia coli

Share to Molecular Sequence Data

Share to Mutation

Source

Identifiers

PMID: 1644311
DOI: 10.1016/0378-1119(92)90485-8

Provenance

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

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Intragenic complementation between Escherichia coli trp repressors with different defects in the tryptophan-binding pocket.PMID 1644311Read ↗

Mutant tryptophan aporepressors with altered specificities of corepressor recognition.Semantic proximity Read ↗

Analyzing the genetic characteristics of a tryptophan-overproducing Escherichia coli.Semantic proximity Read ↗

Studies of the Escherichia coli Trp repressor binding to its five operators and to variant operator sequences.Semantic proximity Read ↗

Enhanced operator binding by trp superrepressors of Escherichia coli.Semantic proximity Read ↗

Shared operator recognition specificity between Trp repressor and the repressors of bacteriophage 434.Semantic proximity Read ↗

Maltose-binding protein interacts simultaneously and asymmetrically with both subunits of the Tar chemoreceptor.Semantic proximity Read ↗

Effect of amino acid alterations in the tryptophan-binding site of the trp repressor.Semantic proximity Read ↗

Mutants in position 69 of the Trp repressor of Escherichia coli K12 with altered DNA-binding specificity.Semantic proximity Read ↗

Characterization of heterodimeric alkaline phosphatases from Escherichia coli: an investigation of intragenic complementation.Semantic proximity Read ↗

Cloning of the trp gene cluster from a tryptophan-hyperproducing strain of Corynebacterium glutamicum: identification of a mutation in the trp leader sequence.Semantic proximity Read ↗

The stereochemistry and biochemistry of the trp repressor-operator complex.Semantic proximity Read ↗

Effects of mutations in the L-tryptophan binding pocket of the Trp RNA-binding attenuation protein of Bacillus subtilis.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.