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The proofreading exonuclease subunit ε of Escherichia coli DNA polymerase III is tethered to the polymerase subunit α via a flexible linker

Ozawa, Kiyoshi; Jergic, Slobodan; Park, Ah Young; Dixon, Nicholas; Otting, Gottfried


Escherichia coli DNA polymerase III holoenzyme is composed of 10 different subunits linked by noncovalent interactions. The polymerase activity resides in the α-subunit. The ε-subunit, which contains the proofreading exonuclease site within its N-terminal 185 residues, binds to α via a segment of 57 additional C-terminal residues, and also to θ, whose function is less well defined. The present study shows that θ greatly enhances the solubility of ε during cell-free synthesis. In addition,...[Show more]

CollectionsANU Research Publications
Date published: 2008-07-28
Type: Journal article
Source: Nucleic Acids Research
DOI: 10.1093/nar/gkn489


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