Abstract:
:DNA damage tolerance (DDT) is responsible for genomic stability and cell viability by bypassing the replication block. In Saccharomyces cerevisiae DDT employs two parallel branch pathways to bypass the DNA lesion, namely translesion DNA synthesis (TLS) and error-free lesion bypass, which are mediated by sequential modifications of PCNA. Rad5 has been placed in the error-free branch of DDT because it contains an E3 ligase domain required for PCNA polyubiquitination. Rad5 is a multi-functional protein and may also play a role in TLS, since it interacts with the TLS polymerase Rev1. In this study we mapped the Rev1-interaction domain in Rad5 to the amino acid resolution and demonstrated that Rad5 is indeed involved in TLS possibly through recruitment of Rev1. Genetic analyses show that the dual functions of Rad5 can be separated and reconstituted. Crystal structure analysis of the Rad5-Rev1 interaction reveals a consensus RFF motif in the Rad5 N-terminus that binds to a hydrophobic pocket within the C-terminal domain of Rev1 that is highly conserved in eukaryotes. This study indicates that Rad5 plays a critical role in pathway choice between TLS and error-free DDT.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Xu X,Lin A,Zhou C,Blackwell SR,Zhang Y,Wang Z,Feng Q,Guan R,Hanna MD,Chen Z,Xiao Wdoi
10.1093/nar/gkw183subject
Has Abstractpub_date
2016-06-20 00:00:00pages
5231-45issue
11eissn
0305-1048issn
1362-4962pii
gkw183journal_volume
44pub_type
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