| Literature DB >> 33087275 |
Muwen Kong1, Emily C Beckwitt2, Bennett Van Houten3.
Abstract
DNA repair is a highly dynamic process in which the actual damage recognition process occurs through an amazing dance between the DNA duplex containing the lesion and the DNA repair proteins. Single molecule investigations have revealed that DNA repair proteins solve the speed-stability paradox, of rapid search versus stable complex formation, by conformational changes induced in both the damaged DNA and the repair proteins. Using Rad4, XPA, PARP1, APE1, OGG1 and UV-DDB as examples, we have discovered how these repair proteins limit their travel on DNA, once a lesion is encountered through a process of anomalous diffusion. We have also observed how PARP1 and APE1, as well as UV-DDB and OGG1 or APE1, co-localize dynamically at sites near DNA damage. This review highlights how our group has greatly benefited from our productive collaborations with Sam Wilson's research group.Entities:
Keywords: APE1; Base excision repair; Nucleotide excision repair; OGG1; PARP1; Single molecule; UV-DDB; XPA; XPC
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Year: 2020 PMID： 33087275 PMCID： PMC7586736 DOI： 10.1016/j.dnarep.2020.102909
Source DB: PubMed Journal: DNA Repair (Amst) ISSN： 1568-7856