Asset Details
Do you wish to reserve the book?
Interplay between human DNA repair proteins at a unique double-strand break in vivo
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?
Interplay between human DNA repair proteins at a unique double-strand break in vivo
Do you wish to request the book?
Interplay between human DNA repair proteins at a unique double-strand break in vivo
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
Interplay between human DNA repair proteins at a unique double-strand break in vivo
2006
Overview
DNA repair by homologous recombination is essential for preserving genomic integrity. The RAD51 paralogs (RAD51B, RAD51C, RAD51D, XRCC2 and XRCC3) play important roles in this process. In this study, we show that human RAD51 interacts with RAD51C‐XRCC3 or RAD51B‐C‐D‐XRCC2. In addition to being critical for RAD51 focus formation, RAD51C localizes to DNA damage sites. Inhibition of RAD51C results in a decrease in cellular proliferation consistent with a role in repairing double‐strand breaks (DSBs) that occur naturally. To monitor a single DNA repair event, we developed immunofluorescence and chromatin immunoprecipitation (ChIP) methods on human cells where a unique DSB can be created
in vivo
. Using this system, we observed a single focus of RAD51C, RAD51 and 53BP1, which colocalized with γ‐H2AX. ChIPs revealed that endogenous human RAD51, RAD51C, RAD51D, XRCC2, XRCC3 and MRE11 proteins are recruited in the S–G2 phase of the cell cycle, while Ku80 is recruited during G1. We propose that RAD51C ensures a tight regulation of RAD51 assembly during DSB repair and plays a direct role in repairing DSBs
in vivo
.
Publisher
John Wiley & Sons, Ltd,Nature Publishing Group UK,Springer Nature B.V
Subject
/ Chromatin Immunoprecipitation
/ DNA
/ DNA-Binding Proteins - analysis
/ DNA-Binding Proteins - antagonists & inhibitors
/ DNA-Binding Proteins - genetics
/ DNA-Binding Proteins - metabolism
/ EMBO13
/ Humans
/ Intracellular Signaling Peptides and Proteins - analysis
/ Intracellular Signaling Peptides and Proteins - metabolism
/ Phosphoproteins - metabolism
/ RAD51
/ Rad51 Recombinase - analysis
/ Rad51 Recombinase - genetics
