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Open AccessArticle

Thermococcus Eurythermalis Endonuclease IV Can Cleave Various Apurinic/Apyrimidinic Site Analogues in ssDNA and dsDNA

1
State Key Laboratory of Microbial Metabolism, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, 800 Dong-Chuan Road, Shanghai 200240, China
2
Shanghai Institute of Applied Physics, Chinese Academy of Sciences, No. 239 Zhangheng Road, Shanghai 201204, China
3
State Key Laboratory of Ocean Engineering, School of Naval Architecture, Ocean and Civil Engineering, Shanghai Jiao Tong University, 800 Dong-Chuan Road, Shanghai 200240, China
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Int. J. Mol. Sci. 2019, 20(1), 69; https://doi.org/10.3390/ijms20010069
Received: 31 October 2018 / Revised: 18 December 2018 / Accepted: 18 December 2018 / Published: 24 December 2018
(This article belongs to the Special Issue DNA Replication Stress)
Endonuclease IV (EndoIV) is a DNA damage-specific endonuclease that mainly hydrolyzes the phosphodiester bond located at 5′ of an apurinic/apyrimidinic (AP) site in DNA. EndoIV also possesses 3′-exonuclease activity for removing 3′-blocking groups and normal nucleotides. Here, we report that Thermococcus eurythermalis EndoIV (TeuendoIV) shows AP endonuclease and 3′-exonuclease activities. The effect of AP site structures, positions and clustered patterns on the activity was characterized. The AP endonuclease activity of TeuendoIV can incise DNA 5′ to various AP site analogues, including the alkane chain Spacer and polyethylene glycol Spacer. However, the short Spacer C2 strongly inhibits the AP endonuclease activity. The kinetic parameters also support its preference to various AP site analogues. In addition, the efficient cleavage at AP sites requires ≥2 normal nucleotides existing at the 5′-terminus. The 3′-exonuclease activity of TeuendoIV can remove one or more consecutive AP sites at the 3′-terminus. Mutations on the residues for substrate recognition show that binding AP site-containing or complementary strand plays a key role for the hydrolysis of phosphodiester bonds. Our results provide a comprehensive biochemical characterization of the cleavage/removal of AP site analogues and some insight for repairing AP sites in hyperthermophile cells. View Full-Text
Keywords: Thermococcus eurythermalis; endonuclease IV; AP site analogue; spacer; DNA repair Thermococcus eurythermalis; endonuclease IV; AP site analogue; spacer; DNA repair
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MDPI and ACS Style

Wang, W.-W.; Zhou, H.; Xie, J.-J.; Yi, G.-S.; He, J.-H.; Wang, F.-P.; Xiao, X.; Liu, X.-P. Thermococcus Eurythermalis Endonuclease IV Can Cleave Various Apurinic/Apyrimidinic Site Analogues in ssDNA and dsDNA. Int. J. Mol. Sci. 2019, 20, 69. https://doi.org/10.3390/ijms20010069

AMA Style

Wang W-W, Zhou H, Xie J-J, Yi G-S, He J-H, Wang F-P, Xiao X, Liu X-P. Thermococcus Eurythermalis Endonuclease IV Can Cleave Various Apurinic/Apyrimidinic Site Analogues in ssDNA and dsDNA. International Journal of Molecular Sciences. 2019; 20(1):69. https://doi.org/10.3390/ijms20010069

Chicago/Turabian Style

Wang, Wei-Wei; Zhou, Huan; Xie, Juan-Juan; Yi, Gang-Shun; He, Jian-Hua; Wang, Feng-Ping; Xiao, Xiang; Liu, Xi-Peng. 2019. "Thermococcus Eurythermalis Endonuclease IV Can Cleave Various Apurinic/Apyrimidinic Site Analogues in ssDNA and dsDNA" Int. J. Mol. Sci. 20, no. 1: 69. https://doi.org/10.3390/ijms20010069

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