What is it about?
This work is about the DNA-dependent protein kinase catalytic subunit (DNA-PKcs), and it's role in non-homologous end joining (NHEJ), a DNA repair pathway of double-strand breaks (DSBs) in DNA. It deals with recognition of DNA-ends, alone as well as in complex with its partner, Ku protein.
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Why is it important?
The structure-function relationship of DNA-PKcs' mechanism of action in NHEJ is poorly understood. Also, the role of Ku and DNA-PKcs proteins within the DNA-PK heterocomplex are rarely studied. Our results indicate that DNA-PKcs plays an important regulatory role within the complex, apart from being the catalytic subunit for protein phosphorylation/autophosphorylation. Three biologically relevant DNA structures were tested, a blunt, splayed and hairpin DNA ends, using synthetic oligonucleotides.
Perspectives
This work is also important as it deals with the study of protein-DNA non-covalent complexes, using surface-plasmon resonance (SPR) technique.
Dr Marko Haramija
University of Rijeka
Read the Original
This page is a summary of: Terminal DNA structure and ATP influence binding parameters of the DNA-dependent protein kinase at an early step prior to DNA synapsis, Nucleic Acids Research, February 2006, Oxford University Press (OUP),
DOI: 10.1093/nar/gkj504.
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