Asset Details
Do you wish to reserve the book?
Structural and functional insights into the interaction between Ku70/80 and Pol X family polymerases in NHEJ
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Structural and functional insights into the interaction between Ku70/80 and Pol X family polymerases in NHEJ
Do you wish to request the book?
Structural and functional insights into the interaction between Ku70/80 and Pol X family polymerases in NHEJ
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Structural and functional insights into the interaction between Ku70/80 and Pol X family polymerases in NHEJ
2025
Overview
Non-homologous end joining (NHEJ) is the main repair pathway for double-strand DNA breaks (DSBs) in mammals. DNA polymerases lambda (Pol λ) and mu (Pol μ), members of the Pol X family, play a key role in this process. However, their interaction within the NHEJ complexes is unclear. Here, we present cryo-EM structures of Pol λ in complex with the DNA-PK long-range synaptic complex, and Pol μ bound to Ku70/80-DNA. These structures identify interaction sites between Ku70/80 and Pol X BRCT domains. Using mutants at the proteins interface in functional assays including cell transfection with an original gap-filling reporter, we define the role of the BRCT domain in the recruitment and activity of the two Pol X members in NHEJ and in their contribution to cell survival following DSBs. Finally, we propose a unified model for the interaction of all Pol X members with Ku70/80.
The molecular basis for the enrollment of X family DNA polymerases in non-homologous end joining (NHEJ) is unclear. Here the authors elucidate the structure of Pol λ within the DNA-PK long-range complex and Pol μ in association with Ku70/80 and characterize the interaction between the BRCT domains of Pol λ and μ with Ku70/80.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 631/80
/ 82/16
/ 82/29
/ 82/80
/ 82/83
/ Biochemistry, Molecular Biology
/ DNA
/ DNA Polymerase beta - chemistry
/ DNA Polymerase beta - genetics
/ DNA Polymerase beta - metabolism
/ DNA Polymerase beta - ultrastructure
/ DNA-Binding Proteins - metabolism
/ DNA-dependent protein kinase
/ DNA-Directed DNA Polymerase - chemistry
/ DNA-Directed DNA Polymerase - genetics
/ DNA-Directed DNA Polymerase - metabolism
/ DNA-Directed DNA Polymerase - ultrastructure
/ Humanities and Social Sciences
/ Humans
/ Ku Autoantigen - ultrastructure
/ Science
