ArticleBiochemistry2008
DNA-dependent conformational changes in the Ku heterodimer.
Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
22 citing papers in PubMed, 39 citations in OpenAlex.
- SETD4-mediated KU70 methylation suppresses apoptosis.Cell reports · 2022Article
- Ycs4 Subunit ofBiochemistry · 2021Article
- SAP domain forms a flexible part of DNA aperture in Ku70/80.The FEBS journal · 2021Article
- The Ku complex: recent advances and emerging roles outside of non-homologous end-joining.Cellular and molecular life sciences : CMLS · 2021Review
- Targeting actin inhibits repair of doxorubicin-induced DNA damage: a novel therapeutic approach for combination therapy.Cell death & disease · 2019Article
- The role of ubiquitin-dependent segregase p97 (VCP or Cdc48) in chromatin dynamics after DNA double strand breaks.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Protection of Arabidopsis Blunt-Ended Telomeres Is Mediated by a Physical Association with the Ku Heterodimer.The Plant cell · 2017Article
- An Intrinsically Disordered APLF Links Ku, DNA-PKcs, and XRCC4-DNA Ligase IV in an Extended Flexible Non-homologous End Joining Complex.The Journal of biological chemistry · 2016Article
- C-terminal region of bacterial Ku controls DNA bridging, DNA threading and recruitment of DNA ligase D for double strand breaks repair.Nucleic acids research · 2016Article
- A moonlighting function of Mycobacterium smegmatis Ku in zinc homeostasis?Protein science : a publication of the Protein Society · 2015Article
- Recognition of DNA Termini by the C-Terminal Region of the Ku80 and the DNA-Dependent Protein Kinase Catalytic Subunit.PloS one · 2015Article
- Repair of double-strand breaks by end joining.Cold Spring Harbor perspectives in biology · 2013Review
- Integration of DNA damage and repair with murine double-minute 2 (Mdm2) in tumorigenesis.International journal of molecular sciences · 2012Review
- Reversion of the ErbB malignant phenotype and the DNA damage response.Experimental and molecular pathology · 2012Review
- Mapping protein surface accessibility via an electron transfer dissociation selectively cleavable hydrazone probe.Molecular & cellular proteomics : MCP · 2012Article
- Computational studies on full-length Ku70 with DNA duplexes: base interactions and a helical path.Journal of molecular modeling · 2012Article
- Multiple protein-protein interactions within the DNA-PK complex are mediated by the C-terminus of Ku 80.International journal of biochemistry and molecular biology · 2012Article
- Review
- Drosophila SAF-B links the nuclear matrix, chromosomes, and transcriptional activity.PloS one · 2010Article
- Molecular analysis of Ku redox regulation.BMC molecular biology · 2009Article
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
Abstract
Ionizing radiation induces DNA double-strand breaks which are repaired by the nonhomologous end joining (NHEJ) pathway. NHEJ is initiated upon Ku binding to the DNA ends and facilitating an interaction with the DNA-dependent protein kinase catalytic subunit (DNA-PKcs). This heterotrimeric DNA-PK complex is then active as a serine/threonine protein kinase. The molecular mechanisms involved in DNA-PK activation are unknown. Considering the crucial role of Ku in this process, we therefore determined the influence of DNA binding on the structure of the Ku heterodimer. Chemical modification with NHS-biotin and mass spectrometry were used to identify sites of modification. Biotinylation of free Ku revealed several reactive lysines on Ku70 and Ku80 which were reduced or eliminated upon DNA binding. Interestingly, in the predicted C-terminal SAP domain of Ku70, biotinylation patterns were observed which suggest a structural change in this region of the protein induced by DNA binding. Limited proteolytic digests of free and DNA-bound Ku revealed a series of unique peptides, again, indicative of a change in the accessibility of the Ku70 and Ku80 C-terminal domains. A 10 kDa peptide was also identified which was preferentially generated under non-DNA-bound conditions and mapped to the C-terminus of Ku70. These results indicate a DNA-dependent movement or structural change in the C-terminal domains of Ku70 and Ku80 that may contribute to DNA-PKcs binding and activation. These results represent the first demonstration of DNA-induced changes in Ku structure and provide a framework for analysis of DNA-PKcs and the mechanism of DNA-PK activation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.