Structural Basis for Novel Interactions between Human TLS Polymerases and PCNA
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- HISHIKI Asami
- Graduate School of Nanobioscience, Yokohama City University
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- HASHIMOTO Hiroshi
- Graduate School of Nanobioscience, Yokohama City University
Bibliographic Information
- Other Title
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- 損傷乗り越え型DNAポリメラーゼとPCNAの相互作用
- 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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Description
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.
Journal
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- Nihon Kessho Gakkaishi
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Nihon Kessho Gakkaishi 51 (5), 286-291, 2009
The Crystallographic Society of Japan
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Details 詳細情報について
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- CRID
- 1390001204086713600
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- NII Article ID
- 10026107483
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- NII Book ID
- AN00188364
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- COI
- 1:CAS:528:DC%2BD1MXhsFSgtbzK
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- ISSN
- 18845576
- 03694585
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- NDL BIB ID
- 10484253
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
- KAKEN
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- Abstract License Flag
- Disallowed