Structural highlights
Function
DPO4_SACS2 Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. It is involved in translesional synthesis.
Publication Abstract from PubMed
The intrinsic l-DNA binding properties of a natural DNA polymerase was discovered. The binding affinity of Dpo4 polymerase for l-DNA was comparable to that for d-DNA. The crystal structure of Dpo4/l-DNA complex revealed a dimer formed by the little finger domain that provides a binding site for l-DNA.
The crystal structure of a natural DNA polymerase complexed with mirror DNA.,An J, Choi J, Hwang D, Park J, Pemble CW 4th, Duong THM, Kim KR, Ahn H, Chung HS, Ahn DR Chem Commun (Camb). 2020 Feb 18;56(14):2186-2189. doi: 10.1039/c9cc09351f. Epub, 2020 Jan 23. PMID:31971182[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ An J, Choi J, Hwang D, Park J, Pemble CW 4th, Duong THM, Kim KR, Ahn H, Chung HS, Ahn DR. The crystal structure of a natural DNA polymerase complexed with mirror DNA. Chem Commun (Camb). 2020 Feb 18;56(14):2186-2189. PMID:31971182 doi:10.1039/c9cc09351f
