Ontology highlight
ABSTRACT:
SUBMITTER: Matsui I
PROVIDER: S-EPMC4187176 | biostudies-literature | 2013 Jul
REPOSITORIES: biostudies-literature
Matsui Ikuo I Matsui Eriko E Yamasaki Kazuhiko K Yokoyama Hideshi H
Life (Basel, Switzerland) 20130705 3
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 subuni ...[more]