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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Yurieva, Olga Georgescu, Roxana E. Yao, Nina Y. Langston, Lance D. Indiani, Chiara Zhang, Dan O'donnell, Mike E. Finkelstein, Jeff |
| Description | Author Affiliation: Langston LD ( The Rockefeller University, Howard Hughes Medical Institute, New York, NY 10065); Zhang D ( The Rockefeller University, Howard Hughes Medical Institute, New York, NY 10065); Yurieva O ( The Rockefeller University, Howard Hughes Medical Institute, New York, NY 10065); Georgescu RE ( The Rockefeller University, Howard Hughes Medical Institute, New York, NY 10065); Finkelstein J ( The Rockefeller University, Howard Hughes Medical Institute, New York, NY 10065); Yao NY ( The Rockefeller University, Howard Hughes Medical Institute, New York, NY 10065); Indiani C ( Manhattan College, Riverdale, NY 10471.); O'Donnell ME ( The Rockefeller University, Howard Hughes Medical Institute, New York, NY 10065); |
| Abstract | DNA replication in eukaryotes is asymmetric, with separate DNA polymerases (Pol) dedicated to bulk synthesis of the leading and lagging strands. Pol /primase initiates primers on both strands that are extended by Pol ε on the leading strand and by Pol δ on the lagging strand. The CMG (Cdc45-MCM-GINS) helicase surrounds the leading strand and is proposed to recruit Pol ε for leading-strand synthesis, but to date a direct interaction between CMG and Pol ε has not been demonstrated. While purifying CMG helicase overexpressed in yeast, we detected a functional complex between CMG and native Pol ε. Using pure CMG and Pol ε, we reconstituted a stable 15-subunit CMG-Pol ε complex and showed that it is a functional polymerase-helicase on a model replication fork in vitro. On its own, the Pol2 catalytic subunit of Pol ε is inefficient in CMG-dependent replication, but addition of the Dpb2 protein subunit of Pol ε, known to bind the Psf1 protein subunit of CMG, allows stable synthesis with CMG. Dpb2 does not affect Pol δ function with CMG, and thus we propose that the connection between Dpb2 and CMG helps to stabilize Pol ε on the leading strand as part of a 15-subunit leading-strand holoenzyme we refer to as CMGE. Direct binding between Pol ε and CMG provides an explanation for specific targeting of Pol ε to the leading strand and provides clear mechanistic evidence for how strand asymmetry is maintained in eukaryotes. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 43 |
| Volume Number | 111 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2014-10-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | DNA Polymerase II Metabolism DNA Replication Holoenzymes Protein Subunits Saccharomyces Cerevisiae Enzymology Chromatography, Gel DNA Helicases Isolation & Purification DNA, Circular Models, Biological Saccharomyces Cerevisiae Proteins Substrate Specificity Time Factors Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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