Publication Abstract from PubMed
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 approximately 70 amino-acid region is folded. The structure consists of a four-alpha-helix bundle including a short parallel beta-sheet, which is similar to the N-terminal regions of the B subunits of human DNA polymerases alpha and epsilon, 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.
Solution structure of the N-terminal domain of the archaeal D-family DNA polymerase small subunit reveals evolutionary relationship to eukaryotic B-family polymerases.,Yamasaki K, Urushibata Y, Yamasaki T, Arisaka F, Matsui I FEBS Lett. 2010 Aug 4;584(15):3370-5. Epub 2010 Jun 23. PMID:20598295[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
