DNA binding and helicase domains of the Escherichia coli recombination protein RecG.
Nucleic Acids Res
; 25(19): 3875-80, 1997 Oct 01.
Article
en En
| MEDLINE
| ID: mdl-9380511
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.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas Bacterianas
/
ADN Bacteriano
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ADN Helicasas
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Proteínas de Escherichia coli
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Escherichia coli
Idioma:
En
Revista:
Nucleic Acids Res
Año:
1997
Tipo del documento:
Article
Pais de publicación:
Reino Unido