Life | |
Domain Structures and Inter-Domain Interactions Defining the Holoenzyme Architecture of Archaeal D-Family DNA Polymerase | |
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;
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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
【 授权许可】
CC BY
© 2013 by the authors; licensee MDPI, Basel, Switzerland.
【 预 览 】
Files | Size | Format | View |
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RO202003190034953ZK.pdf | 660KB | download |