Abstract:
:Rad18 is a ubiquitin E3 ligase that monoubiquitinates PCNA on stalled replications forks. This allows recruitment of damage-tolerant polymerases for damage bypass and DNA repair. In this activity, the Rad18 protein has to interact with Rad6, the E2 ubiquitin-conjugating enzyme, ubiquitin, PCNA and DNA. Here we analyze the biochemical interactions of specific domains of the Rad18 protein. We found that the Rad6/Rad18 complex forms stable dimers in vitro. Consistent with previous findings, both the Ring domain and a C-terminal region contribute to the Rad6 interaction, while the C-terminus is not required for the interaction with PCNA. Surprisingly we find that the C2HC zinc finger is important for interaction with ubiquitin, apparently analogous to the interactions of classical zinc fingers with ubiquitin such as found in the UBZ and UBM domains in Y-family polymerases. Finally we find that the SAP domain, but not the zinc finger domain, is capable of DNA binding in vitro.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Notenboom V,Hibbert RG,van Rossum-Fikkert SE,Olsen JV,Mann M,Sixma TKdoi
10.1093/nar/gkm615subject
Has Abstractpub_date
2007-01-01 00:00:00pages
5819-30issue
17eissn
0305-1048issn
1362-4962pii
gkm615journal_volume
35pub_type
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