書誌事項
- タイトル別名
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- Structural Basis for Novel Interactions between Human TLS Polymerases and PCNA
- ソンショウ ノリコエ ガタ DNA ポリメラーゼ ト PCNA ノ ソウゴ サヨウ
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説明
TransLesion Synthesis (TLS) is a DNA damage tolerance mechanism that allows continued DNA synthesis, even in the presence of damaged DNA templates. In response to DNA damage, TLS polymerases are recruited to replication forks via interactions with ubiquitinated Proliferating Cell Nuclear Antigen (PCNA) involving PCNA-interacting protein box (PIP-box) and ubiquitin-binding domains (UBDs). We now report the first crystal structures of human PCNA in complex with three TLS polymerase peptides containing the non-canonical PIP-box. TLS polymerases interact with PCNA in different ways, both from one another and from canonical PIP-box peptides. Furthermore, we discuss these TLS polymerases interact with ubiquitinated PCNA.
収録刊行物
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- 日本結晶学会誌
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日本結晶学会誌 51 (5), 286-291, 2009
日本結晶学会
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詳細情報 詳細情報について
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- CRID
- 1390001204086713600
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- NII論文ID
- 10026107483
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- NII書誌ID
- AN00188364
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- COI
- 1:CAS:528:DC%2BD1MXhsFSgtbzK
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- ISSN
- 18845576
- 03694585
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- NDL書誌ID
- 10484253
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- NDL
- Crossref
- CiNii Articles
- KAKEN
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- 抄録ライセンスフラグ
- 使用不可
