Solution structure of the N-terminal domain of the archaeal D-family DNA polymerase small subunit reveals evolutionary relationship to eukaryotic B-family polymerases.
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.
Yamasaki
Kazuhiko
K
Biomedical Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), 1-1-1 Higashi, Tsukuba 305-8566, Japan. k-yamasaki@aist.go.jp
Urushibata
Yuji
Y
Yamasaki
Tomoko
T
Arisaka
Fumio
F
Matsui
Ikuo
I
D000251:Adenosine Triphosphatases / Q000737:chemistry; D000595:Amino Acid Sequence; D004259:DNA-Directed DNA Polymerase / Q000737:chemistry*; D056890:Eukaryota / Q000201:enzymology*; D019143:Evolution, Molecular; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D021122:Protein Subunits / Q000737:chemistry*; D043902:Pyrococcus horikoshii / Q000201:enzymology*; D012996:Solutions; D014461:Ultracentrifugation
D021122:Protein Subunits; D012996:Solutions; D004259:DNA-Directed DNA Polymerase; D000251:Adenosine Triphosphatases