title: Domain structures and inter-domain interactions defining the holoenzyme architecture of archaeal d-family DNA polymerase.
abstract: Archaea-specific D-family DNA polymerase (PolD) forms a dimeric heterodimer consisting of two large polymerase subunits and two small exonuclease subunits. According to the protein-protein interactions identified among the domains of large and small subunits of PolD, a symmetrical model for the domain topology of the PolD holoenzyme is proposed. The experimental evidence supports various aspects of the model. The conserved amphipathic nature of the N-terminal putative α-helix of the large subunit plays a key role in the homodimeric assembly and the self-cyclization of the large subunit and is deeply involved in the archaeal PolD stability and activity. We also discuss the evolutional transformation from archaeal D-family to eukaryotic B-family polymerase on the basis of the structural information.
authors.affiliation: Biomedical Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), 1-1-1 Higashi, Tsukuba 305-8566, Japan. ik-matsui@aist.go.jp.
authors.forename: Ikuo
authors.initials: I
authors.lastname: Matsui
authors.affiliation: Biomedical Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), 1-1-1 Higashi, Tsukuba 305-8566, Japan. eriko-matsui@aist.go.jp.
authors.forename: Eriko
authors.initials: E
authors.lastname: Matsui
authors.affiliation: 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.
authors.forename: Kazuhiko
authors.initials: K
authors.lastname: Yamasaki
authors.affiliation: School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka 422-8526, Japan. h-yokoya@u-shizuoka-ken.ac.jp.
authors.forename: Hideshi
authors.initials: H
authors.lastname: Yokoyama