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

Date

2006

Authors

Su, Xun-Cheng
Schaeffer, Patrick
Loscha, Karin
Gan, Pamela
Dixon, Nicholas
Otting, Gottfried

Journal Title

Journal ISSN

Volume Title

Publisher

Blackwell Publishing Ltd

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.

Description

Keywords

Keywords: bacterial DNA; DNA primase; DnaG primase; helicase; primer RNA; single stranded DNA; unclassified drug; article; carboxy terminal sequence; crystal structure; DNA helix; DNA replication; Escherichia coli; Geobacillus stearothermophilus; nonhuman; nuclear DnaB; DnaG; Domain swap; NMR structure; Primase

Citation

Source

The FEBS Journal

Type

Journal article

Book Title

Entity type

Access Statement

License Rights

DOI

10.1111/j.1742-4658.2006.05495.x

Restricted until

2037-12-31