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Life 2013, 3(3), 375-385; doi:10.3390/life3030375

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

1
Biomedical Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), 1-1-1 Higashi, Tsukuba 305-8566, Japan
2
School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka 422-8526, Japan
*
Author to whom correspondence should be addressed.
Received: 15 April 2013 / Revised: 26 June 2013 / Accepted: 27 June 2013 / Published: 5 July 2013
(This article belongs to the Special Issue Extremophiles and Extreme Environments)
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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. View Full-Text
Keywords: D-family DNA polymerase; DNA replication; binding domain; molecular structure; hyperthermophilic archaea; Pyrococcus D-family DNA polymerase; DNA replication; binding domain; molecular structure; hyperthermophilic archaea; Pyrococcus
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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MDPI and ACS Style

Matsui, I.; Matsui, E.; Yamasaki, K.; Yokoyama, H. Domain Structures and Inter-Domain Interactions Defining the Holoenzyme Architecture of Archaeal D-Family DNA Polymerase. Life 2013, 3, 375-385.

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