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- W3183217085 abstract "Abstract Faithful genome duplication requires appropriately controlled replication origin firing. The metazoan Treslin/TICRR origin firing factor and its yeast orthologue Sld3 are regulation hubs of origin firing. They share the Sld3-Treslin domain (STD) and the adjacent TopBP1/Dpb11 interaction domain (TDIN). We report a revised domain architecture model of Treslin/TICRR. Complementary protein sequence analyses uncovered Ku70-homologous β-barrel folds in the Treslin/TICRR middle domain (M domain) and in Sld3. Thus, the Sld3-homologous Treslin/TICRR core comprises its three central domains, M domain, STD and TDIN. This Sld3-core is flanked by non-conserved terminal domains, the CIT (conserved in Treslins) and the C-terminus. We also identified Ku70-like β-barrels in MTBP and Sld7. Our binding experiments showed that the Treslin β-barrel mediates interaction with the MTBP β-barrel, reminiscent of the homotypic Ku70-Ku80 dimerization. This binding mode is conserved in the Sld3-Sld7 dimer. We used Treslin/TICRR domain mutants to show that all Sld3-core domains and the non-conserved terminal domains fulfil important functions during origin firing in human cells. Thus, metazoa-specific and widely conserved molecular processes cooperate during origin firing in metazoa." @default.
- W3183217085 created "2021-08-02" @default.
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- W3183217085 date "2021-07-24" @default.
- W3183217085 modified "2023-10-15" @default.
- W3183217085 title "Refining the domain architecture model of the replication origin firing factor Treslin/TICRR" @default.
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- W3183217085 doi "https://doi.org/10.1101/2021.07.24.453613" @default.
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