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

343 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.",

year = "2007",

month = jul,

day = "1",

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

language = "English",

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

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Y1 - 2007/7/1

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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AN - SCOPUS:34249941966

SN - 1568-7864

VL - 6

SP - 891

EP - 899

JO - DNA Repair

JF - DNA Repair

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Translesion synthesis: Y-family polymerases and the polymerase switch

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