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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/DPO4_CALS4 DPO4_CALS4] 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. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. | | [https://www.uniprot.org/uniprot/DPO4_CALS4 DPO4_CALS4] Poorly processive, error-prone DNA polymerase involved in translesion repair and 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 (By similarity). Involved in translesional synthesis. Primer extension fidelity in vitro is temperature-dependent. Inserts a correct base opposite templating bases at 70 degrees Celsius, but at 37 degrees Celsius in addition to correct base pairing, base transitions, transversions and frameshifts can occur. Preferably forms erroneous base pairs C:T. Bypasses 8-oxo-dG oxidative damage by incorporating dATP or dCTP opposite of the damaged DNA template site at both temperatures in vitro (PubMed:37683741).[UniProtKB:Q47155][HAMAP-Rule:MF_01113]<ref>PMID:37683741</ref> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Translesion synthesis (TLS) is a kind of DNA repair that maintains the stability of the genome and ensures the normal growth of life in cells under emergencies. Y-family DNA polymerases, as a kind of error-prone DNA polymerase, mainly perform TLS. Previous studies have suggested that the occurrence of tumors is associated with the overexpression of human DNA polymerase of the Y family. And the combination of Y-family DNA polymerase inhibitors is promising for cancer therapy. Here we report the functional and structural characterization of a member of the Y-family DNA polymerases, TTEDbh. We determine TTEDbh is an extreme TLS polymerase that can cross oxidative damage sites, and further identify the amino acids and novel structures that are critical for DNA binding, synthesis, fidelity, and oxidative damage bypass. Moreover, previously unnoticed structural elements with important functions have been discovered and analyzed. These studies provide a more experimental basis for further elucidating the molecular mechanisms of DNA polymerase in the Y family. It could also shed light on the design of drugs to target tumors.
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| Structure and function of extreme TLS DNA polymerase TTEDbh from Thermoanaerobacter tengcongensis.,Tian LF, Gao H, Yang S, Liu YP, Li M, Xu W, Yan XX Int J Biol Macromol. 2023 Dec 31;253(Pt 2):126770. doi: , 10.1016/j.ijbiomac.2023.126770. Epub 2023 Sep 6. PMID:37683741<ref>PMID:37683741</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 7yll" style="background-color:#fffaf0;"></div>
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| == References == | | == References == |
| <references/> | | <references/> |
