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J Biol Chem, Vol. 274, Issue 28, 19644-19648, July 9, 1999

Specific DNA Recognition by F Factor TraY Involves -Sheet Residues

From the Department of Biology, The Johns Hopkins University, Baltimore, Maryland 21218

The F Factor TraY protein is a sequence-specific DNA-binding protein required for efficient conjugal transfer. Genetic and biochemical studies indicate that TraY has two functional roles in conjugation. TraY binds to the P_Y promoter to up-regulate transcription of tra genes. TraY also binds to the plasmid origin of transfer (oriT), serving as an accessory protein in the nicking of F Factor in preparation for transfer. TraY is thought to belong to the ribbon-helix-helix family of transcription factors. These proteins contact DNA using residues of an antiparallel -sheet. We engineered and characterized six TraY mutants each having a single potential -sheet DNA contact residue replaced with Ala. Most TraY mutants had significantly reduced affinity for the TraY oriT binding site while possessing near wild-type stability and nonspecific DNA recognition. These results indicate that TraY -sheet residues participate in DNA recognition, and support inclusion of TraY in the ribbon-helix-helix family.

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