Dr Gary Sharples gary.sharples@durham.ac.uk
Associate Professor
A mutation in helicase motif III of E. coli RecG protein abolishes branch migration of Holliday junctions.
Sharples, G.J.; Whitby, M.C.; Ryder, L.; Lloyd, R.G.
Authors
M.C. Whitby
L. Ryder
R.G. Lloyd
Abstract
The RecG protein of Escherichia coli catalyses branch migration of Holliday junctions made by RecA and dissociates synthetic X junctions into duplex products in reactions that require hydrolysis of ATP. To investigate the mode of action of this enzyme a chromosomal mutation that inactivates recG (recG162) was cloned and sequenced. The recG162 mutation is a G:C to A:T transition, which produces an Ala428 to Val substitution in the protein. This change affects a motif (motif III) in the protein that is highly conserved in DNA and RNA helicases. RecG162 protein was purified and shown to retain the ability to bind synthetic X and Y junctions. However, it does not dissociate these junctions and fails to catalyse branch migration of Holliday junction intermediates purified from a RecA strand exchange reaction. RecG162 retains a DNA-dependent ATPase activity, but this is much reduced relative to the wild-type protein, especially with single-stranded DNA as a co-factor. These results suggest that branch migration by RecG is related to a junction-targeted DNA helicase activity.
Citation
Sharples, G., Whitby, M., Ryder, L., & Lloyd, R. (1994). A mutation in helicase motif III of E. coli RecG protein abolishes branch migration of Holliday junctions. Nucleic Acids Research, 22(3), 308-313
Journal Article Type | Article |
---|---|
Publication Date | 1994 |
Journal | Nucleic Acids Research |
Print ISSN | 0305-1048 |
Publisher | Oxford University Press |
Volume | 22 |
Issue | 3 |
Pages | 308-313 |
Publisher URL | http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8127666 |
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