1H, 13C, and 15N NMR assignments for the helicase interaction domain of Staphylococcus aureus DnaG primase |
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| Authors: | Matthew D. Shortridge Mark A. Griep Robert Powers |
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| Affiliation: | (1) Department of Chemistry, University of Nebraska-Lincoln, 721 Hamilton Hall, Lincoln, NE 68588-0304, USA;(2) Department of Chemistry, University of Nebraska-Lincoln, 736 Hamilton Hall, Lincoln, NE 68588-0304, USA;(3) Department of Chemistry, University of Nebraska-Lincoln, 722 Hamilton Hall, Lincoln, NE 68588-0304, USA |
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| 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 1H, 13C, and 15N backbone and side-chain resonance assignments for the C-terminal helicase interaction domain of Staphylococcus aureus primase. |
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