著者
菱木 麻美 橋本 博
出版者
日本結晶学会
雑誌
日本結晶学会誌 (ISSN:03694585)
巻号頁・発行日
vol.51, no.5, pp.286-291, 2009-10-31 (Released:2010-12-01)
参考文献数
26

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.
著者
橋本 博 菱木 麻美 原 幸大 菊池 壮太郎
出版者
一般社団法人 日本生物物理学会
雑誌
生物物理 (ISSN:05824052)
巻号頁・発行日
vol.57, no.1, pp.015-019, 2017 (Released:2017-01-26)
参考文献数
20

DNA damage tolerance (DTT) is a cell function to avoid replication arrest by DNA damage during DNA replication. DTT includes two pathways, translesion DNA synthesis (TLS) and template-switched DNA synthesis (TS), regulated by various molecular interactions. TLS is transient DNA synthesis using a damaged template by error-prone DNA polymerases specialized for DNA damage (TLS polymerases). TS, in which one newly synthesized strand is utilized as an undamaged template for replication by replicative polymerases, is error-free process. This review article describes recent progress in structural studies of proteins involved in TLS and TS.