Translesion synthesis: Y-family polymerases and the polymerase switch

Lehmann, Alan R.; Niimi, Atsuko; Ogi, Tomoo; Brown, Stephanie; Sabbioneda, Simone; Wing, Jonathan F.; Kannouche, Patricia; Green, Catherine

doi:10.1016/j.dnarep.2007.02.003

Cited by 346 publications

(415 citation statements)

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“…Mammalian cells contain specialized DNA polymerases (pols) that play important roles in translesion synthesis (TLS) [23,24]. It has been shown that TLS DNA pols bypassed 8-OH-Gua in vitro [25][26][27][28][29][30][31][32][33][34].…”

Section: -Oh-gua Is Highly Mutagenic and Induces G:ct:a Transversiomentioning

confidence: 99%

“…Although the incorporation of 2'-deoxyribonucleotides opposite 8-OH-Gua in template DNA by DNA pol ι in vitro was reported [31][32][33], the result obtained in this study suggests that the contribution of the DNA pol to 8-OH-Gua bypass is minimal, at best, at least in this human cell line. REV1 is a member of the Y-family DNA pols, but it acts as deoxycytidyl transferase opposite a range of damaged bases [23,24]. Human 14 REV1 inserts dCTP opposite 8-OH-Gua in vitro [34].…”

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confidence: 99%

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Roles of specialized DNA polymerases in mutagenesis by 8-hydroxyguanine in human cells

Kamiya

Yamaguchi

Suzuki

et al. 2010

Mutation Research/Fundamental and Molecular Mechanisms of Mutag

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Section: -Oh-gua Is Highly Mutagenic and Induces G:ct:a Transversiomentioning

confidence: 99%

mentioning

confidence: 99%

Roles of specialized DNA polymerases in mutagenesis by 8-hydroxyguanine in human cells

Kamiya

Yamaguchi

Suzuki

et al. 2010

Mutation Research/Fundamental and Molecular Mechanisms of Mutag

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“…In 1999, however, an entirely new category of polymerases was discovered in prokaryotes and eukaryotes [2-4] -the lesion-bypass DNA polymerases. The function of lesion-bypass polymerases is to replicate past lesion-containing DNA templates in a process called translesion synthesis [5][6][7]. Now at least 16 DNA polymerases are known in eukaryotes [8] and five in bacteria [9].…”

Section: Lesions and Dna Polymerasesmentioning

confidence: 99%

“…High-fidelity polymerases are members of the A and B families, whereas the lesion-bypass DNA polymerases belong primarily, but not exclusively, to the Y family. The lesion-bypass DNA polymerases have important roles in the temporary replacement of high-fidelity DNA polymerases that are stalled upon encountering damaged DNA sites, an event termed 'polymerase switch' [5][6][7].…”

Section: The High-fidelity Dna Polymerase Bfmentioning

confidence: 99%

“…Here, RNA polymerases provide a potential link: bulky lesions such as those derived from BP [51] cause RNA polymerase stalling, which invokes the transcription-coupled nucleotide excision repair (NER) machinery [52,53], but much remains to be learned about relationships between lesion structure and repair susceptibility by this machinery [54]. Understanding lesion-processing in cells will require the elucidation of concerted interactions between Y-family DNA polymerases with other polymerases and other components of the holoenzyme replication complex; the participation of other proteins such as the eukaryotic ubiquitylation machinery also must be further explicated [6,7,[55][56][57]. To fully decipher how high-fidelity and lesion-bypass DNA polymerases correct the plethora of possible DNA lesions, structural and biochemical information will be needed on a case-bycase basis.…”

Section: Concluding Remarks and Future Perspectivesmentioning

confidence: 99%

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Lesion processing: high-fidelity versus lesion-bypass DNA polymerases

Broyde¹,

Wang²,

Rechkoblit³

et al. 2008

Trends in Biochemical Sciences

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When a high-fidelity DNA polymerase encounters certain DNA-damage sites, its progress can be stalled and one or more lesion-bypass polymerases are recruited to transit the lesion. Here, we consider two representative types of lesions: (i) 7,8-dihydro-8-oxogua-nine (8-oxoG), a small, highly prevalent lesion caused by oxidative damage; and (ii) bulky lesions derived from the environmental pre-carcinogen benzo [a]pyrene, in the high-fidelity DNA polymerase Bacillus fragment (BF) from Bacillus stearothermophilus and in the lesion-bypass DNA polymerase IV (Dpo4) from Sulfolobus solfataricus. The tight fit of the BF polymerase around the nascent base pair contrasts with the more spacious, solvent-exposed active site of Dpo4, and these differences in architecture result in distinctions in their respective functions: one-step versus stepwise polymerase translocation, mutagenic versus accurate bypass of 8-oxoG, and polymerase stalling versus mutagenic bypass at bulky benzo[a]pyrene-derived lesions. Lesions and DNA polymerasesUntil 1999, it was widely understood that bacteria have three DNA polymerases and mammals have five [1]. In 1999, however, an entirely new category of polymerases was discovered in prokaryotes and eukaryotes [2-4] -the lesion-bypass DNA polymerases. The function of lesion-bypass polymerases is to replicate past lesion-containing DNA templates in a process called translesion synthesis [5][6][7]. Now at least 16 DNA polymerases are known in eukaryotes [8] and five in bacteria [9]. Furthermore, since 1999, crystal structures of DNA polymerases, including those containing lesions, have provided new structural insights into the mechanistic aspects of translesion synthesis and polymerase stalling associated with DNA lesions. For a review of the structures and mechanisms of DNA polymerases up to the year 2005, see Ref.[10].Here, we discuss the structural and functional features of representative high-fidelity and lesion-bypass DNA polymerases (Box 1) and how these features affect the processing of certain forms of DNA damage. The lesions considered are derived from reactions of intermediates produced by endogenous sources or from the metabolic activation of environmental genotoxic

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The interaction between ubiquitin and yeast polymerase η C terminus does not require the UBZ domain

et al. 2020

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Edited by Claus AzzalinPolymerase g (Polg) is one of the Y-family polymerases that is recruited by monoubiquitinated proliferating cell nuclear antigen (Ub-PCNA) to DNA damage sites during translesion synthesis (TLS). This interaction is mediated by an ubiquitin-binding zinc-finger (UBZ) domain and a PCNA-interacting protein (PIP) box in Polg, which binds to ubiquitin and PCNA, respectively. Here, we show that without the UBZ domain, the PIP box of yeast Polg has a novel binding function with ubiquitin. Furthermore, the UBZ domain and the PIP box share the same binding surfaces for ubiquitin. The interaction with ubiquitin via the PIP box stabilizes the Ub-PCNA/Polg complex. Moreover, the PIP residues I624 and L625 contribute to Polg function in TLS in vivo.

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Translesion synthesis: Y-family polymerases and the polymerase switch

Cited by 346 publications

References 96 publications

Roles of specialized DNA polymerases in mutagenesis by 8-hydroxyguanine in human cells

Roles of specialized DNA polymerases in mutagenesis by 8-hydroxyguanine in human cells

Lesion processing: high-fidelity versus lesion-bypass DNA polymerases

The interaction between ubiquitin and yeast polymerase η C terminus does not require the UBZ domain

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