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Tunability of DNA Polymerase Stability during Eukaryotic DNA Replication

Journal Article


Abstract


  • © 2019 Elsevier Inc. Structural and biochemical studies have revealed the basic principles of how the replisome duplicates genomic DNA, but little is known about its dynamics during DNA replication. We reconstitute the 34 proteins needed to form the S. cerevisiae replisome and show how changing local concentrations of the key DNA polymerases tunes the ability of the complex to efficiently recycle these proteins or to dynamically exchange them. Particularly, we demonstrate redundancy of the Pol α-primase DNA polymerase activity in replication and show that Pol α-primase and the lagging-strand Pol δ can be re-used within the replisome to support the synthesis of large numbers of Okazaki fragments. This unexpected malleability of the replisome might allow it to deal with barriers and resource challenges during replication of large genomes.

UOW Authors


  •   Lewis, Jacob S. (external author)
  •   Spenkelink, Lisanne
  •   Schauer, Grant (external author)
  •   Yurieva, Olga (external author)
  •   Mueller, Stefan (external author)
  •   Natarajan, Varsha (external author)
  •   Kaur, Gurleen (external author)
  •   Maher, Claire (external author)
  •   Kay, Callum (external author)
  •   O'Donnell, Michael (external author)
  •   van Oijen, Antoine M.

Publication Date


  • 2020

Citation


  • Lewis, J., Spenkelink, L., Schauer, G., Yurieva, O., Mueller, S., Natarajan, V., Kaur, G., Maher, C., Kay, C., O'Donnell, M. & van Oijen, A. (2020). Tunability of DNA Polymerase Stability during Eukaryotic DNA Replication. Molecular Cell, 77 (1), 17-25.

Scopus Eid


  • 2-s2.0-85076931598

Ro Metadata Url


  • http://ro.uow.edu.au/smhpapers1/1089

Has Global Citation Frequency


Number Of Pages


  • 8

Start Page


  • 17

End Page


  • 25

Volume


  • 77

Issue


  • 1

Place Of Publication


  • United States

Abstract


  • © 2019 Elsevier Inc. Structural and biochemical studies have revealed the basic principles of how the replisome duplicates genomic DNA, but little is known about its dynamics during DNA replication. We reconstitute the 34 proteins needed to form the S. cerevisiae replisome and show how changing local concentrations of the key DNA polymerases tunes the ability of the complex to efficiently recycle these proteins or to dynamically exchange them. Particularly, we demonstrate redundancy of the Pol α-primase DNA polymerase activity in replication and show that Pol α-primase and the lagging-strand Pol δ can be re-used within the replisome to support the synthesis of large numbers of Okazaki fragments. This unexpected malleability of the replisome might allow it to deal with barriers and resource challenges during replication of large genomes.

UOW Authors


  •   Lewis, Jacob S. (external author)
  •   Spenkelink, Lisanne
  •   Schauer, Grant (external author)
  •   Yurieva, Olga (external author)
  •   Mueller, Stefan (external author)
  •   Natarajan, Varsha (external author)
  •   Kaur, Gurleen (external author)
  •   Maher, Claire (external author)
  •   Kay, Callum (external author)
  •   O'Donnell, Michael (external author)
  •   van Oijen, Antoine M.

Publication Date


  • 2020

Citation


  • Lewis, J., Spenkelink, L., Schauer, G., Yurieva, O., Mueller, S., Natarajan, V., Kaur, G., Maher, C., Kay, C., O'Donnell, M. & van Oijen, A. (2020). Tunability of DNA Polymerase Stability during Eukaryotic DNA Replication. Molecular Cell, 77 (1), 17-25.

Scopus Eid


  • 2-s2.0-85076931598

Ro Metadata Url


  • http://ro.uow.edu.au/smhpapers1/1089

Has Global Citation Frequency


Number Of Pages


  • 8

Start Page


  • 17

End Page


  • 25

Volume


  • 77

Issue


  • 1

Place Of Publication


  • United States