title: ¹H, ¹³C, and ¹⁵N NMR assignments for the helicase interaction domain of Staphylococcus aureus DnaG primase.
abstract: The interaction between DnaG primase and DnaB helicase is essential for stimulating primer synthesis during bacterial DNA replication. The interaction occurs between the N-terminal domain of helicase and the C-terminal domain of primase. Here we present the (1)H, (13)C, and (15)N backbone and side-chain resonance assignments for the C-terminal helicase interaction domain of Staphylococcus aureus primase.
authors.affiliation: Department of Chemistry, University of Nebraska-Lincoln, 721 Hamilton Hall, Lincoln, NE 68588-0304, USA. mds8575@huskers.unl.edu
authors.forename: Matthew D
authors.initials: MD
authors.lastname: Shortridge
authors.forename: Mark A
authors.initials: MA
authors.lastname: Griep
authors.forename: Robert
authors.initials: R
authors.lastname: Powers
mesh_terms: D004265:DNA Helicases / Q000378:metabolism*; D019915:DNA Primase / Q000737:chemistry* / Q000378:metabolism*; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D012996:Solutions; D013211:Staphylococcus aureus / Q000201:enzymology*
chemical_list: D012996:Solutions; D019915:DNA Primase; D004265:DNA Helicases