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research
Cellular location and activity of Escherichia coli RecG proteins shed light on the function of its structurally unresolved C-terminus
Authors
Abd Wahab
Akeel A. Mahdi
+67Β more
Al-Deib
Amy L. Upton
Atkinson
Bachmann
Bernhardt
Bolt
Brendler
Briggs
Briggs
Buss
Christian J. Rudolph
Datsenko
David S. Milner
Gari
Geoffrey S. Briggs
Gregg
Gupta
Hong
Jaktaji
Jane I. Grove
Lau
Lecointe
Lesterlin
Lia
Lloyd
Lloyd
Lloyd
Machwe
Mahdi
Mahdi
Mahdi
Mahdi
Manosas
Marians
McGlynn
McGlynn
McGlynn
McGlynn
McGlynn
McGlynn
McGlynn
Michel
Parsons
Pomerantz
Ralf
Robert G. Lloyd
Rocha
Rudolph
Rudolph
Rudolph
Rudolph
Seigneur
Sharples
Shereda
Singleton
Sun
Trautinger
Tsaneva
Vincent
Waldminghaus
West
Whitby
Whitby
Whitby
Whitby
Zacharias
Zhang
Publication date
1 April 2014
Publisher
'Oxford University Press (OUP)'
Doi
Cite
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on
PubMed
Abstract
RecG is a DNA translocase encoded by most species of bacteria. The Escherichia coli protein targets branched DNA substrates and drives the unwinding and rewinding of DNA strands. Its ability to remodel replication forks and to genetically interact with PriA protein have led to the idea that it plays an important role in securing faithful genome duplication. Here we report that RecG co-localises with sites of DNA replication and identify conserved arginine and tryptophan residues near its C-terminus that are needed for this localisation. We establish that the extreme C-terminus, which is not resolved in the crystal structure, is vital for DNA unwinding but not for DNA binding. Substituting an alanine for a highly conserved tyrosine near the very end results in a substantial reduction in the ability to unwind replication fork and Holliday junction structures but has no effect on substrate affinity. Deleting or substituting the terminal alanine causes an even greater reduction in unwinding activity, which is somewhat surprising as this residue is not uniformly present in closely related RecG proteins. More significantly, the extreme C-terminal mutations have little effect on localisation. Mutations that do prevent localisation result in only a slight reduction in the capacity for DNA repair. Β© 2014 The Author(s)
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info:doi/10.1093%2Fnar%2Fgku22...
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