DNA-Dependent Conformational Changes in the Ku Heterodimer

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 com...

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Published inBiochemistry (Easton) Vol. 47; no. 15; pp. 4359 - 4368
Main Authors Lehman, Jason A, Hoelz, Derek J, Turchi, John J
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 15.04.2008
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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.
AbstractList 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.
Ionizing radiation induces DNA double-strand breaks which are repaired by the non-homologous 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 was 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-terminus 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 Ku70 C-terminus. 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.
Author Lehman, Jason A
Hoelz, Derek J
Turchi, John J
AuthorAffiliation Biomedical Sciences Graduate Program, Wright State University, Dayton, Ohio 45435
Department of Biochemistry & Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana 46202
Department of Medicine, Indiana University School of Medicine, Indianapolis, Indiana 46202
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– name: Department of Medicine, Indiana University School of Medicine, Indianapolis, Indiana 46202
– name: Department of Biochemistry & Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana 46202
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  start-page: 971
  year: 2005
  ident: ref27/cit27
  publication-title: Biochemistry
  doi: 10.1021/bi048208a
  contributor:
    fullname: Shell S. M.
SSID ssj0004074
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Snippet Ionizing radiation induces DNA double-strand breaks which are repaired by the nonhomologous end joining (NHEJ) pathway. NHEJ is initiated upon Ku binding to...
Ionizing radiation induces DNA double-strand breaks which are repaired by the non-homologous end joining (NHEJ) pathway. NHEJ is initiated upon Ku binding to...
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SubjectTerms Amino Acid Sequence
Antigens, Nuclear - chemistry
Biotinylation
Dimerization
DNA - chemistry
DNA-Binding Proteins - chemistry
Humans
Ku Autoantigen
Ligands
Lysine - chemistry
Mass Spectrometry
Models, Molecular
Molecular Sequence Data
Peptides - chemistry
Protein Binding
Protein Structure, Tertiary
Solvents - chemistry
Title DNA-Dependent Conformational Changes in the Ku Heterodimer
URI http://dx.doi.org/10.1021/bi702284c
https://api.istex.fr/ark:/67375/TPS-HLR2XBJ1-3/fulltext.pdf
https://www.ncbi.nlm.nih.gov/pubmed/18355052
https://search.proquest.com/docview/70489805
https://pubmed.ncbi.nlm.nih.gov/PMC2432109
Volume 47
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