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The unstructured C-terminus of the τ subunit of Escherichia coli DNA polymerase III holoenzyme is the site of interaction with the α subunit

Jergic, Slobodan; Ozawa, Kiyoshi; Williams, Neal; Su, Xun-Cheng; Scott, Daniel; Hamdan, Samir; Crowther, Jeffrey; Dixon, Nicholas; Otting, Gottfried


The τ subunit of Escherichia coli DNA polymerase III holoenzyme interacts with the α subunit through its C-terminal Domain V,τC16. We show that the extreme C-terminal region of τC16 constitutes the site of interaction with α. The τC16 domain, but not a derivative of it with a C-terminal deletion of seven residues (τC16∆7), forms an isolable complex with α. Surface plasmon resonance measurements were used to determine the dissociation constant (KD) of the α–τC16 complex to be ~260 pM....[Show more]

CollectionsANU Research Publications
Date published: 2007-03-13
Type: Journal article
Source: Nucleic Acids Research
DOI: 10.1093/nar/gkm079


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