Monomeric solution structure of the helicase-binding domain of Escherichia coli DnaG primase

Journal Publication ResearchOnline@JCU
Su, Xun-Cheng;Schaeffer, Patrick M.;Loscha, Karin V.;Gan, Pamela H. P.;Dixon, Nicholas E. ;Otting, Gottfried
Abstract

DnaG is the primase that lays down RNA primers on single-stranded DNA during bacterial DNA replication. The solution structure of the DnaB-helicase-binding C-terminal domain of Escherichia coli DnaG was determined by NMR spectroscopy at near-neutral pH. The structure is a rare fold that, besides occurring in DnaG C-terminal domains, has been described only for the N-terminal domain of DnaB. The C-terminal helix hairpin present in the DnaG C-terminal domain, however, is either less stable or absent in DnaB, as evidenced by high mobility of the C-terminal 35 residues in a construct comprising residues 1–171. The present structure identifies the previous crystal structure of the E. coli DnaG C-terminal domain as a domain-swapped dimer. It is also significantly different from the NMR structure reported for the corresponding domain of DnaG from the thermophile Bacillus stearothermophilus. NMR experiments showed that the DnaG C-terminal domain does not bind to residues 1–171 of the E. coli DnaB helicase with significant affinity.

Journal

FEBS Journal

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Volume

273

ISBN/ISSN

1742-4658

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Issue

21

Pages Count

13

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Publisher

Wiley-Blackwell

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N/A

DOI

10.1111/j.1742-4658.2006.05495.x