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Solution structure of the N‐terminal domain of the archaeal D‐family DNA polymerase small subunit reveals evolutionary relationship to eukaryotic B‐family polymerases
Author(s) -
Yamasaki Kazuhiko,
Urushibata Yuji,
Yamasaki Tomoko,
Arisaka Fumio,
Matsui Ikuo
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.06.026
Subject(s) - heterotetramer , dna polymerase , polymerase , protein subunit , biology , primer (cosmetics) , dna clamp , genetics , biochemistry , dna , chemistry , rna , reverse transcriptase , gene , organic chemistry
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.