Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis

被引:575
|
作者
Bienko, M
Green, CM
Crosetto, N
Rudolf, F
Zapart, G
Coull, B
Kannouche, P
Wider, G
Peter, M
Lehmann, AR
Hofmann, K
Dikic, I
机构
[1] Univ Frankfurt, Sch Med, Inst Biochem 2, D-60590 Frankfurt, Germany
[2] Univ Sussex, Brighton BN1 9RQ, E Sussex, England
[3] ETH Honggerberg, Inst Mol Biol & Biophys, CH-8093 Zurich, Switzerland
[4] Miltenyi Biotec GmbH, Bioinformat Grp, D-50829 Cologne, Germany
关键词
D O I
10.1126/science.1120615
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Translesion synthesis (TLS) is the major pathway by which mammalian cells replicate across DNA lesions. Upon DNA damage, ubiquitination of proliferating cell nuclear antigen (PCNA) induces bypass of the lesion by directing the replication machinery into the TLS pathway. Yet, how this modification is recognized and interpreted in the cell remains unclear. Here we describe the identification of two ubiquitin (Ub)-binding domains (UBM and UBZ), which are evolutionarily conserved in all Y-family TLS polymerases (pols). These domains are required for binding of pol eta and pol iota to ubiquitin, their accumulation in replication factories, and their interaction with monoubiquitinated PCNA. Moreover, the UBZ domain of poll) is essential to efficiently restore a normal response to ultraviolet irradiation in xeroderma pigmentosum variant (XP-V) fibroblasts. Our results indicate that Ub-binding domains of Y-family polymerases play crucial regulatory roles in TLS.
引用
收藏
页码:1821 / 1824
页数:4
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