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• W2118873017 startingPage "22283" @default.
• W2118873017 abstract "As first observed by Wittenberg (Kesti, T., Flick, K., Keranen, S., Syvaoja, J. E., and Wittenburg, C. (1999)Mol. Cell 3, 679–685), we find that deletion mutants lacking the entire N-terminal DNA polymerase domain of yeast pol e are viable. However, we now show that point mutations in DNA polymerase catalytic residues of pol e are lethal. Taken together, the phenotypes of the deletion and the point mutants suggest that the polymerase of pol e may normally participate in DNA replication but that another polymerase can substitute in its complete absence. Substitution is inefficient because the deletion mutants have serious defects in DNA replication. This observation raises the question of what is the essential function of the C-terminal half of pol e. We show that the ability of the C-terminal half of the polymerase to support growth is disrupted by mutations in the cysteine-rich region, which disrupts both dimerization of the POL2 gene product and interaction with the essential DPB2 subunit, suggesting that this region plays an important architectural role at the replication fork even in the absence of the polymerase function. Finally, the S phase checkpoint, with respect to both induction ofRNR3 transcription and cell cycle arrest, is intact in cells where replication is supported only by the C-terminal half of pol e, but it is disrupted in mutants affecting the cysteine-rich region, suggesting that this domain directly affects the checkpoint rather than acting through the N-terminal polymerase active site." @default.
• W2118873017 created "2016-06-24" @default.
• W2118873017 creator A5000378293 @default.
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• W2118873017 date "1999-08-01" @default.
• W2118873017 modified "2023-10-12" @default.
• W2118873017 title "Analysis of the Essential Functions of the C-terminal Protein/Protein Interaction Domain of Saccharomyces cerevisiae pol ε and Its Unexpected Ability to Support Growth in the Absence of the DNA Polymerase Domain" @default.
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• W2118873017 doi "https://doi.org/10.1074/jbc.274.32.22283" @default.
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