Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2049048 | FEBS Letters | 2010 | 6 Pages |
Abstract
Archaea-specific D-family DNA polymerase forms a heterotetramer consisting of two large polymerase subunits and two small exonuclease subunits. We analyzed the structure of the N-terminal 200 amino-acid regulatory region of the small subunit by NMR and revealed that the N-terminal ∼70 amino-acid region is folded. The structure consists of a four-α-helix bundle including a short parallel β-sheet, which is similar to the N-terminal regions of the B subunits of human DNA polymerases α and ε, establishing evolutionary relationships among these archaeal and eukaryotic polymerases. We observed monomer–dimer equilibrium of this domain, which may be related to holoenzyme architecture and/or functional regulation.
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Authors
Kazuhiko Yamasaki, Yuji Urushibata, Tomoko Yamasaki, Fumio Arisaka, Ikuo Matsui,