%0 Journal Article
%T Domain Structures and Inter-Domain Interactions Defining the Holoenzyme Architecture of Archaeal D-Family DNA Polymerase
%A Ikuo Matsui
%A Eriko Matsui
%A Kazuhiko Yamasaki
%A Hideshi Yokoyama
%J Life
%D 2013
%I MDPI AG
%R 10.3390/life3030375
%X 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 ¦Á-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.
%K D-family DNA polymerase
%K DNA replication
%K binding domain
%K molecular structure
%K hyperthermophilic archaea
%K Pyrococcus
%U http://www.mdpi.com/2075-1729/3/3/375