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Mutant Trp repressors with new DNA-binding specificities.

S Bass¹, V Sorrells, P Youderian

¹Department of Biological Sciences, University of Southern California, Los Angeles 90089-1481.

Science (New York, N.Y.)

|October 14, 1988

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Mutations in the Escherichia coli tryptophan aporepressor (Trp repressor) reveal Thr81

Area of Science:

Molecular Biology
Genetics
Biochemistry

Background:

The Escherichia coli trpR gene encodes the tryptophan aporepressor (Trp repressor).
The Trp repressor regulates tryptophan biosynthesis by binding to specific DNA operator sequences.
Understanding repressor-operator interactions is crucial for gene regulation studies.

Purpose of the Study:

To investigate the role of specific amino acid residues in the Trp repressor's DNA binding specificity.
To elucidate the molecular mechanisms underlying Trp repressor-operator interactions.
To compare the DNA binding strategies of Trp repressor with other related DNA-binding proteins.

Main Methods:

Oligonucleotide-directed mutagenesis was employed to generate 36 mutant Trp repressors.

Related Experiment Videos

Mutant repressors were tested for binding affinity to 28 different operator sequences.

Comparative analysis of binding specificities between wild-type and mutant repressors.

Main Results:

Eleven of the 36 mutant repressors exhibited altered binding profiles.
Five mutants displayed novel binding specificities, indicating key roles for specific residues.
The hydroxyl and methyl groups of Threonine-81 (Thr81) were identified as critical for operator recognition.

Conclusions:

Threonine-81 (Thr81) plays a dual role in Trp repressor-operator binding specificity.
Isoleucine-79 (Ile79) and Alanine-80 (Ala80) do not appear to mediate sequence-specific DNA contacts.
The Trp repressor's in vivo DNA interaction mechanism differs significantly from those of phage lambda and 434 repressors.