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. 1991 May;128(1):29–35. doi: 10.1093/genetics/128.1.29

Mutant Tryptophan Aporepressors with Altered Specificities of Corepressor Recognition

D N Arvidson 1, M Shapiro 1, P Youderian 1
PMCID: PMC1204450  PMID: 2060777

Abstract

The Escherichia coli trpR gene encodes tryptophan aporepressor, which binds the corepressor ligand, L-tryptophan, to form an active repressor complex. The side chain of residue valine 58 of Trp aporepressor sits at the bottom of the corepressor (L-tryptophan) binding pocket. Mutant trpR genes encoding changes of Val(58) to the other 19 naturally occurring amino acids were made. Each of the mutant proteins requires a higher intracellular concentration of tryptophan for activation of DNA binding than wild-type aporepressor. Whereas wild-type aporepressor is activated better by 5-methyltryptophan (5-MT) than by tryptophan, Ile(58) and other mutant aporepressors prefer tryptophan to 5-MT as corepressor, and Ala(58) and Gly(58) prefer 5-MT much more strongly than wild-type aporepressor in vivo. These mutant aporepressors are the first examples of DNA-binding proteins with altered specificities of cofactor recognition.

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Selected References

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