scholarly journals Genetic and physical interactions between Polη and Rev1 in response to UV-induced DNA damage in mammalian cells

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Tonghui Bi ◽  
Xiaohong Niu ◽  
Chunping Qin ◽  
Wei Xiao

AbstractIn response to UV irradiation, translesion DNA synthesis (TLS) utilizes specialized DNA polymerases to bypass replication-blocking lesions. In a well-established polymerase switch model, Polη is thought to be a preferred TLS polymerase to insert correct nucleotides across from the thymine dimer, and Rev1 plays a scaffold role through physical interaction with Polη and the Rev7 subunit of Polζ for continual DNA synthesis. Defective Polη causes a variant form of xeroderma pigmentosum (XPV), a disease with predisposition to sunlight-induced skin cancer. Previous studies revealed that expression of Rev1 alone is sufficient to confer enhanced UV damage tolerance in mammalian cells, which depends on its physical interaction with Polζ but is independent of Polη, a conclusion that appears to contradict current literature on the critical roles of Polη in TLS. To test a hypothesis that the Rev1 catalytic activity is required to backup Polη in TLS, we found that the Rev1 polymerase-dead mutation is synergistic with either Polη mutation or the Polη-interaction mutation in response to UV-induced DNA damage. On the other hand, functional complementation of polH cells by Polη relies on its physical interaction with Rev1. Hence, our studies reveal critical interactions between Rev1 and Polη in response to UV damage.

2022 ◽  
Vol 8 ◽  
Author(s):  
Denisse Carvajal-Maldonado ◽  
Lea Drogalis Beckham ◽  
Richard D. Wood ◽  
Sylvie Doublié

DNA polymerases catalyze nucleotidyl transfer, the central reaction in synthesis of DNA polynucleotide chains. They function not only in DNA replication, but also in diverse aspects of DNA repair and recombination. Some DNA polymerases can perform translesion DNA synthesis, facilitating damage tolerance and leading to mutagenesis. In addition to these functions, many DNA polymerases conduct biochemically distinct reactions. This review presents examples of DNA polymerases that carry out nuclease (3ʹ—5′ exonuclease, 5′ nuclease, or end-trimming nuclease) or lyase (5′ dRP lyase) extracurricular activities. The discussion underscores how DNA polymerases have a remarkable ability to manipulate DNA strands, sometimes involving relatively large intramolecular movement.


2011 ◽  
Vol 192 (2) ◽  
pp. 219-227 ◽  
Author(s):  
Thomas Göhler ◽  
Simone Sabbioneda ◽  
Catherine M. Green ◽  
Alan R. Lehmann

DNA polymerase η (polη) belongs to the Y-family of DNA polymerases and facilitates translesion synthesis past UV damage. We show that, after UV irradiation, polη becomes phosphorylated at Ser601 by the ataxia-telangiectasia mutated and Rad3-related (ATR) kinase. DNA damage–induced phosphorylation of polη depends on its physical interaction with Rad18 but is independent of PCNA monoubiquitination. It requires the ubiquitin-binding domain of polη but not its PCNA-interacting motif. ATR-dependent phosphorylation of polη is necessary to restore normal survival and postreplication repair after ultraviolet irradiation in xeroderma pigmentosum variant fibroblasts, and is involved in the checkpoint response to UV damage. Taken together, our results provide evidence for a link between DNA damage–induced checkpoint activation and translesion synthesis in mammalian cells.


PLoS ONE ◽  
2019 ◽  
Vol 14 (3) ◽  
pp. e0213383 ◽  
Author(s):  
Masataka Tsuda ◽  
Saki Ogawa ◽  
Masato Ooka ◽  
Kaori Kobayashi ◽  
Kouji Hirota ◽  
...  

2007 ◽  
Vol 402 (2) ◽  
pp. 321-329 ◽  
Author(s):  
Giuseppina Blanca ◽  
Emmanuelle Delagoutte ◽  
Nicolas Tanguy le gac ◽  
Neil P. Johnson ◽  
Giuseppe Baldacci ◽  
...  

Replicative DNA polymerases, such as T4 polymerase, possess both elongation and 3′–5′ exonuclease proofreading catalytic activities. They arrest at the base preceding DNA damage on the coding DNA strand and specialized DNA polymerases have evolved to replicate across the lesion by a process known as TLS (translesion DNA synthesis). TLS is considered to take place in two steps that often require different enzymes, insertion of a nucleotide opposite the damaged template base followed by extension from the inserted nucleotide. We and others have observed that inactivation of the 3′–5′ exonuclease function of T4 polymerase enables TLS across a single site-specific abasic [AP (apurinic/apyrimidinic)] lesion. In the present study we report a role for auxiliary replicative factors in this reaction. When replication is performed with a large excess of DNA template over DNA polymerase in the absence of auxiliary factors, the exo− polymerase (T4 DNA polymerase deficient in the 3′–5′ exonuclease activity) inserts one nucleotide opposite the AP site but does not extend past the lesion. Addition of the clamp processivity factor and the clamp loader complex restores primer extension across an AP lesion on a circular AP-containing DNA substrate by the exo− polymerase, but has no effect on the wild-type enzyme. Hence T4 DNA polymerase exhibits a variety of responses to DNA damage. It can behave as a replicative polymerase or (in the absence of proofreading activity) as a specialized DNA polymerase and carry out TLS. As a specialized polymerase it can function either as an inserter or (with the help of accessory proteins) as an extender. The capacity to separate these distinct functions in a single DNA polymerase provides insight into the biochemical requirements for translesion DNA synthesis.


2014 ◽  
Vol 5 (1) ◽  
Author(s):  
Omer Ziv ◽  
Amit Zeisel ◽  
Nataly Mirlas-Neisberg ◽  
Umakanta Swain ◽  
Reinat Nevo ◽  
...  

Acta Naturae ◽  
2017 ◽  
Vol 9 (3) ◽  
pp. 12-26 ◽  
Author(s):  
А. V. Ignatov ◽  
K. A. Bondarenko ◽  
A. V. Makarova

DNA damage is a major cause of replication interruption, mutations, and cell death. DNA damage is removed by several types of repair processes. The involvement of specialized DNA polymerases in replication provides an important mechanism that helps tolerate persistent DNA damage. Specialized DNA polymerases incorporate nucleotides opposite lesions with high efficiency but demonstrate low accuracy of DNA synthesis. In this review, we summarize the types and mechanisms of formation and repair of non-bulky DNA lesions, and we provide an overview of the role of specialized DNA polymerases in translesion DNA synthesis.


2005 ◽  
Vol 19 (1) ◽  
pp. 143
Author(s):  
Errol C. Friedberg ◽  
Alan R. Lehmann ◽  
Robert P.P. Fuchs

2011 ◽  
Vol 286 (37) ◽  
pp. 32094-32104 ◽  
Author(s):  
Giuseppe Villani ◽  
Ulrich Hubscher ◽  
Nadege Gironis ◽  
Sinikka Parkkinen ◽  
Helmut Pospiech ◽  
...  

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