Translesion synthesis

Translesion synthesis can bypass a replication block caused by various DNA damage. Specialised translesion synthesis DNA polymerases can replicate DNA over such lesions to resume publication but the enzymes are error prone.

Latest Research and Reviews

Research | 04 February 2019 | open

A cancer-associated point mutation disables the steric gate of human PrimPol
- Alberto Díaz-Talavera
- , Patricia A. Calvo
- , Daniel González-Acosta
- , Marcos Díaz
- , Guillermo Sastre-Moreno
- , Luis Blanco-Franco
- , Susana Guerra
- , Maria I. Martínez-Jiménez
- , Juan Méndez
- & Luis Blanco
Scientific Reports 9, 1121
Research | 31 January 2019 | open

AKT inhibition impairs PCNA ubiquitylation and triggers synthetic lethality in homologous recombination-deficient cells submitted to replication stress
- Florencia Villafañez
- , Iris Alejandra García
- , Sofia Carbajosa
- , María Florencia Pansa
- , Sabrina Mansilla
- , María Candelaria Llorens
- , Virginia Angiolini
- , Laura Guantay
- , Heinz Jacobs
- , Kevin P. Madauss
- , Israel Gloger
- , Vanesa Gottifredi
- , Jose Luis Bocco
- & Gaston Soria
Oncogene, 1-15
Research | 09 July 2018 | open

The active site residues Gln55 and Arg73 play a key role in DNA damage bypass by S. cerevisiae Pol η
- Elizaveta O. Boldinova
- , Artem Ignatov
- , Andrey Kulbachinskiy
- & Alena V. Makarova
Scientific Reports 8, 10314
Research | 18 December 2017 | open

Single-molecule imaging reveals multiple pathways for the recruitment of translesion polymerases after DNA damage

Translesion synthesis (TLS) enables cells to tolerate damaged DNA encountered during replication. Here the authors use super-resolution photoactivation localization microscopy to reveal a lesion type dependent mechanism of recruitment of the TLS polymerase Pol IV following DNA damage.
- Elizabeth S. Thrall
- , James E. Kath
- , Seungwoo Chang
- & Joseph J. Loparo
Nature Communications 8, 2170
Research | 05 December 2017 | open

Polη O-GlcNAcylation governs genome integrity during translesion DNA synthesis

Polη is a key player in translesion DNA synthesis. Here, the authors uncover that, in response to DNA damage, Polη undergoes O-GlcNAcylation at threonine 457 by O-GlcNAc transferase to facilitate the timely disassembly of Polη after DNA lesion bypass.
- Xiaolu Ma
- , Hongmei Liu
- , Jing Li
- , Yihao Wang
- , Yue-He Ding
- , Hongyan Shen
- , Yeran Yang
- , Chenyi Sun
- , Min Huang
- , Yingfeng Tu
- , Yang Liu
- , Yongliang Zhao
- , Meng-Qiu Dong
- , Ping Xu
- , Tie-Shan Tang
- & Caixia Guo
Nature Communications 8, 1941
Research | 16 October 2017 | open

Collision with duplex DNA renders Escherichia coli DNA polymerase III holoenzyme susceptible to DNA polymerase IV-mediated polymerase switching on the sliding clamp
- Thanh Thi Le
- , Asako Furukohri
- , Masahiro Tatsumi-Akiyama
- & Hisaji Maki
Scientific Reports 7, 12755

All Research & Reviews

News and Comment

Research Highlights | 05 April 2017

DNA Damage Response: RNA m⁶A regulates DNA repair
- Eytan Zlotorynski
Nature Reviews Molecular Cell Biology 18, 277
Research Highlights | 14 December 2015

DNA replication: Quad-jumping
- Eytan Zlotorynski
Nature Reviews Genetics 17, 67
Research Highlights | 09 December 2015

DNA replication: Quad-jumping

The primase–polymerase PrimPol is required for bypassing G-quadruplexes in vertebrate cells by repriming replication downstream of the structures.
- Eytan Zlotorynski
Nature Reviews Molecular Cell Biology 17, 2-3
Comments and Opinion | 04 November 2015

A DNA-hairpin model for repeat-addition processivity in telomere synthesis

Telomerase is a nucleoprotein complex of a reverse transcriptase and an RNA that binds complementary telomeric-repeat DNA sequences and directs their extension. In this Commentary, the authors propose how hairpin structures formed by telomeric DNA repeats promote addition of telomerase repeats and why telomere sequences are evolutionarily conserved despite the problems that they pose to DNA replication.
- Wei Yang
- & Young-Sam Lee
Nature Structural & Molecular Biology 22, 844-847
Editorial | 04 November 2015

Unraveling the ends

Deciphering the complexity of events at telomeres has enhanced understanding of how telomeres function to maintain genome integrity and how their dysfunction gives rise to human disease.

Nature Structural & Molecular Biology 22, 843
News and Views | 04 December 2013

PrimPol breaks replication barriers

Faithful bypass of replication forks encountering obstructive DNA lesions is essential to prevent fork collapse and cell death. PrimPol is a new human primase and translesion polymerase that is able to bypass fork-blocking UV-induced lesions and to restart replication by origin-independent repriming.
- Thomas Helleday
Nature Structural & Molecular Biology 20, 1348-1350