Rad27 and Exo1 function in different excision pathways for mismatch repair in Saccharomyces cerevisiae

Felipe A. Calil, Bin-Zhong Li, Kendall A. Torres, Katarina Nguyen, Nikki Bowen, Christopher D. Putnam and Richard D. Kolodner ()
Additional contact information
Felipe A. Calil: Ludwig Institute for Cancer Research, University of California School of Medicine
Bin-Zhong Li: Ludwig Institute for Cancer Research, University of California School of Medicine
Kendall A. Torres: Ludwig Institute for Cancer Research, University of California School of Medicine
Katarina Nguyen: Ludwig Institute for Cancer Research, University of California School of Medicine
Nikki Bowen: Ludwig Institute for Cancer Research, University of California School of Medicine
Christopher D. Putnam: Ludwig Institute for Cancer Research, University of California School of Medicine
Richard D. Kolodner: Ludwig Institute for Cancer Research, University of California School of Medicine

Nature Communications, 2021, vol. 12, issue 1, 1-10

Abstract: Abstract Eukaryotic DNA Mismatch Repair (MMR) involves redundant exonuclease 1 (Exo1)-dependent and Exo1-independent pathways, of which the Exo1-independent pathway(s) is not well understood. The exo1Δ440-702 mutation, which deletes the MutS Homolog 2 (Msh2) and MutL Homolog 1 (Mlh1) interacting peptides (SHIP and MIP boxes, respectively), eliminates the Exo1 MMR functions but is not lethal in combination with rad27Δ mutations. Analyzing the effect of different combinations of the exo1Δ440-702 mutation, a rad27Δ mutation and the pms1-A99V mutation, which inactivates an Exo1-independent MMR pathway, demonstrated that each of these mutations inactivates a different MMR pathway. Furthermore, it was possible to reconstitute a Rad27- and Msh2-Msh6-dependent MMR reaction in vitro using a mispaired DNA substrate and other MMR proteins. Our results demonstrate Rad27 defines an Exo1-independent eukaryotic MMR pathway that is redundant with at least two other MMR pathways.

Date: 2021
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-021-25866-z Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-25866-z

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-021-25866-z

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().