The interaction between ubiquitin and yeast polymerase eta C terminus does not require the UBZ domain

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Polymerase eta (Pol eta) 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 Pol eta, which binds to ubiquitin and PCNA, respectively. Here, we show that without the UBZ domain, the PIP box of yeast Pol eta 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/Pol eta complex. Moreover, the PIP residues I624 and L625 contribute to Pol eta function in TLS in vivo.
Publisher
WILEY
Issue Date
2020-06
Language
English
Article Type
Article
Citation

FEBS LETTERS, v.594, no.11, pp.1726 - 1737

ISSN
0014-5793
DOI
10.1002/1873-3468.13783
URI
http://hdl.handle.net/10203/275342
Appears in Collection
CH-Journal Papers(저널논문)BS-Journal Papers(저널논문)
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