Telomere proteins POT1, TRF1 and TRF2 augment long-patch base excision repair in vitro.

Cell Cycle
Adam S MillerRobert A Bambara

Abstract

Human telomeres consist of multiple tandem hexameric repeats, each containing a guanine triplet. Guanosine-rich clusters are highly susceptible to oxidative base damage, necessitating base excision repair (BER). Previous demonstration of enhanced strand displacement synthesis by the BER component DNA polymerase β in the presence of telomere protein TRF2 suggests that telomeres employ long-patch (LP) BER. Earlier analyses in vitro showed that efficiency of BER reactions is reduced in the DNA-histone environment of chromatin. Evidence presented here indicates that BER is promoted at telomeres. We found that the three proteins that contact telomere DNA, POT1, TRF1 and TRF2, enhance the rate of individual steps of LP-BER and stimulate the complete reconstituted LP-BER pathway. Thought to protect telomere DNA from degradation, these proteins still apparently evolved to allow selective access of repair proteins.

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Citations

Oct 16, 2013·Proceedings of the National Academy of Sciences of the United States of America·Sibylle MadlenerNurten Saydam
Jul 31, 2012·Free Radical Biology & Medicine·Nazmul HudaDavid Gilley
Oct 1, 2015·DNA Repair·Pingping JiaWeihang Chai
Dec 4, 2015·Annual Review of Genetics·Kin Chan, Dmitry A Gordenin
Apr 8, 2014·Journal of Molecular Biology·Mengxia LiDavid M Wilson
May 2, 2014·DNA Repair·Susan S Wallace
May 29, 2016·DNA Repair·Elise FouquerelPatricia Opresko
May 12, 2018·Nucleic Acids Research·Mengxia LiDavid M Wilson
Jul 3, 2019·Frontiers in Neurology·Yanjun TianYili Wu
Aug 23, 2019·The Journal of Biological Chemistry·Borja Barbero Barcenilla, Dorothy E Shippen
Apr 4, 2021·Biology·Graciela Gavia-GarcíaVíctor Manuel Mendoza-Núñez
Oct 29, 2020·Seminars in Cell & Developmental Biology·Elisa BalzanoSimona Giunta

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