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Nucleic Acids Research, Vol 25, Issue 19 3875-3880, Copyright © 1997 by Oxford University Press

ARTICLES

DNA binding and helicase domains of the Escherichia coli recombination protein RecG

AA Mahdi, P McGlynn, SD Levett and RG Lloyd
Department of Genetics, University of Nottingham, Queens Medical Centre, Nottingham NG7 2UH, UK.

The Escherichia coli RecG protein is a unique junction-specific helicase involved in DNA repair and recombination. The C-terminus of RecG contains motifs conserved throughout a wide range of DNA and RNA helicases and it is thought that this C-terminal half of RecG contains the helicase active site. However, the regions of RecG which confer junction DNA specificity are unknown. To begin to assign structure- function relationships within RecG, a series of N- and C-terminal deletions have been engineered into the protein, together with an N- terminal histidine tag fusion peptide for purification purposes. Junction DNA binding, unwinding and ATP hydrolysis were disrupted by mutagenesis of the N-terminus. In contrast, C-terminal deletions moderately reduced junction DNA binding but almost abolished unwinding. These data suggest that the C-terminus does contain the helicase active site whereas the N-terminus confers junction DNA specificity.
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