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나노물질 및 화학반응 연구단
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The interaction between ubiquitin and yeast polymerase η C terminus does not require the UBZ domain

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Title
The interaction between ubiquitin and yeast polymerase η C terminus does not require the UBZ domain
Author(s)
Phuong Thi Mai Duong; Anh Thi Ngoc Bui; Seong-Ok Kim; Hee-Sung Park; Yeon-Soo Seo; Byong-Seok Choi
Subject
monoubiquitinated PCNA, ; polymerase η, ; translesion synthesis, ; ubiquitin-binding, ; UBZ
Publication Date
2020-06
Journal
FEBS LETTERS, v.594, no.11, pp.1726 - 1737
Publisher
ELSEVIER SCIENCE BV
Abstract
© 2020 Federation of European Biochemical Societies. Polymerase η (Polη) is one of the Y-family polymerases that is recruited by monoubiquitinated proliferating cell nuclear antigen (Ub-PCNA) to DNA damage sites during translesion synthesis (TLS). This interaction is mediated by an ubiquitin-binding zinc-finger (UBZ) domain and a PCNA-interacting protein (PIP) box in Polη, which binds to ubiquitin and PCNA, respectively. Here, we show that without the UBZ domain, the PIP box of yeast Polη has a novel binding function with ubiquitin. Furthermore, the UBZ domain and the PIP box share the same binding surfaces for ubiquitin. The interaction with ubiquitin via the PIP box stabilizes the Ub-PCNA/Polη complex. Moreover, the PIP residues I624 and L625 contribute to Polη function in TLS in vivo
URI
https://pr.ibs.re.kr/handle/8788114/7848
DOI
10.1002/1873-3468.13783
ISSN
0014-5793
Appears in Collections:
Center for Nanomaterials and Chemical Reactions(나노물질 및 화학반응 연구단) > 1. Journal Papers (저널논문)
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