PMID:9380511
| Citation |
Mahdi, AA, McGlynn, P, Levett, SD and Lloyd, RG (1997) DNA binding and helicase domains of the Escherichia coli recombination protein RecG. Nucleic Acids Res. 25:3875-80 |
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| Abstract |
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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| Keywords |
Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Base Sequence; Binding Sites/genetics; DNA Helicases/metabolism; DNA Repair; DNA, Bacterial/genetics; DNA, Bacterial/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Genes, Bacterial; Histidine/chemistry; Peptide Fragments/chemistry; Peptide Fragments/genetics; Peptide Fragments/metabolism; Protein Binding; Protein Engineering; Recombination, Genetic; Sequence Deletion; Sequence Tagged Sites |
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