Browse views: by Year, by Function, by GLF, by Subfunction, by Conference, by Journal

Study of the ATP-binding site of helicase IV from Escherichia coli.

Dubaele, Sandy, Lourdel, Claude and Chene, Patrick (2006) Study of the ATP-binding site of helicase IV from Escherichia coli. Biochemical and Biophysical Research Communications, 341 (3). pp. 828-836. ISSN 0006-291X


Helicases contain conserved motifs involved in ATP/magnesium/nucleic acid binding and in the mechanisms coupling nucleotide hydrolysis to duplex unwinding. None of these motifs are located at the adenine-binding pocket of the protein. We show here that the superfamily I helicase, helicase IV from Escherichia coli, utilizes a conserved glutamine and conserved aromatic residue to interact with ATP. Other superfamily I helicases such as, UvrD/Rep/PcrA also possess these residues but in addition they interact with adenine via a conserved arginine, which is replaced by a serine in helicase IV. Mutation of this serine residue in helicase IV into histidine or methionine leads to proteins with unaffected ATPase and DNA-binding activities but with low helicase activity. This suggests that residues located at the adenine-binding pocket, in addition to be involved in ATP-binding, are important for efficient coupling between ATP hydrolysis and DNA unwinding.

Item Type: Article
Related URLs:
Additional Information: author can archive post-print (ie final draft post-refereeing); Publisher's version/PDF cannot be used
Keywords: Helicase; Helicase IV; Q motif; ATPase; Uncoupling
Related URLs:
Date Deposited: 14 Dec 2009 14:00
Last Modified: 31 Jan 2013 01:17


Email Alerts

Register with OAK to receive email alerts for saved searches.