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Expression, purification, crystallization, and NMR studies of the helicase interaction domain of Escherichia coli DnaG primase

Loscha, Karin; Oakley, Aaron; Bancia, Bogdan; Schaeffer, Patrick; Prosselkov, Pavel; Wilce, Matthew; Dixon, Nicholas; Otting, Gottfried

Description

In Escherichia coli, the DnaG primase is the RNA polymerase that synthesizes RNA primers at replication forks. It is composed of three domains, a small N-terminal zinc-binding domain, a larger central domain responsible for RNA synthesis, and a C-terminal domain comprising residues 434-581 [DnaG(434-581)] that interact with the hexameric DnaB helicase. Presumably because of this interaction, it had not been possible previously to express the C-terminal domain in a stably transformed E. coli...[Show more]

CollectionsANU Research Publications
Date published: 2004
Type: Journal article
URI: http://hdl.handle.net/1885/77892
Source: Protein Expression and Purification
DOI: 10.1016/j.pep.2003.10.001

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