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

研究成果: ジャーナルへの寄稿 › 学術論文 › 査読

331 被引用数 (Scopus)

抄録

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.

本文言語	英語
ページ（範囲）	891-899
ページ数	9
ジャーナル	DNA Repair
巻	6
号	7
DOI	https://doi.org/10.1016/j.dnarep.2007.02.003
出版ステータス	出版済み - 01-07-2007
外部発表	はい

All Science Journal Classification (ASJC) codes

生化学
分子生物学
細胞生物学

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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.",

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. Copyright: Copyright 2009 Elsevier B.V., All rights reserved.",

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AU - Brown, Stephanie

AU - Sabbioneda, Simone

AU - Wing, Jonathan F.

AU - Kannouche, Patricia L.

AU - Green, Catherine M.

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N2 - 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.

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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Translesion synthesis: Y-family polymerases and the polymerase switch

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