Translesion synthesis: Y-family polymerases and the polymerase switch

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

doi:10.1016/j.dnarep.2007.02.003

Translesion synthesis: Y-family polymerases and the polymerase switch

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

Research output: Contribution to journal › Article › peer-review

333 Citations (Scopus)

Abstract

Replicative DNA polymerases are blocked at DNA lesions. Synthesis past DNA damage requires the replacement of the replicative polymerase by one of a group of specialised translesion synthesis (TLS) polymerases, most of which belong to the Y-family. Each of these has different substrate specificities for different types of damage. In eukaryotes mono-ubiquitination of PCNA plays a crucial role in the switch from replicative to TLS polymerases at stalled forks. All the Y-family polymerases have ubiquitin binding sites that increase their binding affinity for ubiquitinated PCNA at the sites of stalled forks.

Original language	English
Pages (from-to)	891-899
Number of pages	9
Journal	DNA Repair
Volume	6
Issue number	7
DOIs	https://doi.org/10.1016/j.dnarep.2007.02.003
Publication status	Published - 1 Jul 2007

Keywords

DNA polymerase
PCNA
Replication factories
Ubiquitination

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10.1016/j.dnarep.2007.02.003

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title = "Translesion synthesis: Y-family polymerases and the polymerase switch",

abstract = "Replicative DNA polymerases are blocked at DNA lesions. Synthesis past DNA damage requires the replacement of the replicative polymerase by one of a group of specialised translesion synthesis (TLS) polymerases, most of which belong to the Y-family. Each of these has different substrate specificities for different types of damage. In eukaryotes mono-ubiquitination of PCNA plays a crucial role in the switch from replicative to TLS polymerases at stalled forks. All the Y-family polymerases have ubiquitin binding sites that increase their binding affinity for ubiquitinated PCNA at the sites of stalled forks.",

keywords = "DNA polymerase, PCNA, Replication factories, Ubiquitination",

author = "Lehmann, {Alan R.} and Atsuko Niimi and Tomoo Ogi and Stephanie Brown and Simone Sabbioneda and Wing, {Jonathan F.} and Kannouche, {Patricia L.} and Green, {Catherine M.}",

note = "Funding Information: Work on TLS in the authors{\textquoteright} laboratory is supported by the Medical Research Council, European Community, European Science Foundation and Unilever.",

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doi = "10.1016/j.dnarep.2007.02.003",

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T2 - Y-family polymerases and the polymerase switch

AU - Lehmann, Alan R.

AU - Niimi, Atsuko

AU - Ogi, Tomoo

AU - Brown, Stephanie

AU - Sabbioneda, Simone

AU - Wing, Jonathan F.

AU - Kannouche, Patricia L.

AU - Green, Catherine M.

N1 - Funding Information: Work on TLS in the authors’ laboratory is supported by the Medical Research Council, European Community, European Science Foundation and Unilever.

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AB - Replicative DNA polymerases are blocked at DNA lesions. Synthesis past DNA damage requires the replacement of the replicative polymerase by one of a group of specialised translesion synthesis (TLS) polymerases, most of which belong to the Y-family. Each of these has different substrate specificities for different types of damage. In eukaryotes mono-ubiquitination of PCNA plays a crucial role in the switch from replicative to TLS polymerases at stalled forks. All the Y-family polymerases have ubiquitin binding sites that increase their binding affinity for ubiquitinated PCNA at the sites of stalled forks.

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KW - PCNA

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Translesion synthesis: Y-family polymerases and the polymerase switch

Abstract

Keywords

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