The interaction between ubiquitin and yeast polymerase ? C terminus does not require the UBZ domain.
Polymerase ? (Pol?) 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?, which binds to ubiquitin and ... PCNA, respectively. Here, we show that without the UBZ domain, the PIP box of yeast Pol? 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? complex. Moreover, the PIP residues I624 and L625 contribute to Pol? function in TLS in vivo.
Mesh Terms:
Amino Acid Sequence, DNA, DNA Damage, DNA Replication, DNA-Directed DNA Polymerase, Isoleucine, Leucine, Magnetic Resonance Spectroscopy, Models, Molecular, Proliferating Cell Nuclear Antigen, Protein Binding, Protein Domains, Saccharomyces cerevisiae, Ubiquitin, Zinc Fingers
Amino Acid Sequence, DNA, DNA Damage, DNA Replication, DNA-Directed DNA Polymerase, Isoleucine, Leucine, Magnetic Resonance Spectroscopy, Models, Molecular, Proliferating Cell Nuclear Antigen, Protein Binding, Protein Domains, Saccharomyces cerevisiae, Ubiquitin, Zinc Fingers
FEBS Lett
Date: Dec. 01, 2019
PubMed ID: 32239506
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