This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
8ka4
From Proteopedia
Arabidopsis AP endonuclease ARP complex with 21bp THF-containing DNA
Structural highlights
FunctionARP_ARATH Repairs oxidative DNA damages, seems also to act as a redox factor (PubMed:7512729). Is multifunctional and may be involved both in DNA repair and in the regulation of transcription (PubMed:7512729). Exhibits apurinic/apyrimidinic (AP) endonuclease activity (PubMed:21781197, PubMed:25228464, PubMed:25569774). Catalyzes the conversion of 3'-phosphor-alpha,beta-unsaturated aldehyde (3'-PUA) to 3'-OH (PubMed:25228464). May be involved in base excision repair in chloroplasts (PubMed:19372224). According to a report, has a significant in vitro 3'-phosphatase activity (PubMed:25228464). According to another report, has no in vitro 3'-phosphatase activity (PubMed:25569774). Has a strong non-specific affinity to DNA (PubMed:25228464).[1] [2] [3] [4] [5] [6] Publication Abstract from PubMedBase excision repair (BER) is a critical genome defense pathway that copes with a broad range of DNA lesions induced by endogenous or exogenous genotoxic agents. AP endonucleases in the BER pathway are responsible for removing the damaged bases and nicking the abasic sites. In plants, the BER pathway plays a critical role in the active demethylation of 5-methylcytosine (5mC) DNA modification. Here, we have determined the crystal structures of Arabidopsis AP endonuclease AtARP in complex with the double-stranded DNA containing tetrahydrofuran (THF) that mimics the abasic site. We identified the critical residues in AtARP for binding and removing the abasic site and the unique residues for interacting with the orphan base. Additionally, we investigated the differences among the three plant AP endonucleases and evaluated the general DNA repair capacity of AtARP in a mammalian cell line. Our studies provide further mechanistic insights into the BER pathway in plants. Structural insights into the catalytic mechanism of the AP endonuclease AtARP.,Guo W, Wu W, Wen Y, Gao Y, Zhuang S, Meng C, Chen H, Zhao Z, Hu K, Wu B Structure. 2024 Mar 8:S0969-2126(24)00053-4. doi: 10.1016/j.str.2024.02.014. PMID:38503293[7] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
