Domain Structures and Inter-Domain Interactions Defining the Holoenzyme Architecture of Archaeal D-Family DNA Polymerase

Life

Ikuo Matsui¹  Eriko Matsui¹  Kazuhiko Yamasaki¹ 

[1] Biomedical Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), 1-1-1 Higashi, Tsukuba 305-8566, Japan; E-Mails:

关键词: D-family DNA polymerase;    DNA replication;    binding domain;    molecular structure;    hyperthermophilic archaea;    Pyrococcus;   

DOI  :  10.3390/life3030375

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2013 by the authors; licensee MDPI, Basel, Switzerland.