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PMID: 11577093 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Genetic analysis of the DNA-dependent protein kinase reveals an inhibitory role of Ku in late S-G2 phase DNA double-strand break repair.

The Journal of biological chemistry ·Vol. 276 ·No. 48 ·2001-11-30 ·Pages 44413-8

Fukushima T, Takata M, Morrison C, Araki R, Fujimori A, Abe M, Tatsumi K, Jasin M, Dhar PK, Sonoda E, Chiba T, Takeda S

Abstract

Two major complementary double-strand break (DSB) repair pathways exist in vertebrates, homologous recombination (HR), which involves Rad54, and non-homologous end-joining, which requires the DNA-dependent protein kinase (DNA-PK). DNA-PK comprises a catalytic subunit (DNA-PKcs) and a DNA-binding Ku70 and Ku80 heterodimer. To define the activities of individual DNA-PK components in DSB repair, we targeted the DNA-PKcs gene in chicken DT40 cells. DNA-PKcs deficiency caused a DSB repair defect that was, unexpectedly, suppressed by KU70 disruption. We have shown previously that genetic ablation of Ku70 confers RAD54-dependent radioresistance on S-G(2) phase cells, when sister chromatids are available for HR repair. To test whether direct interference by Ku70 with HR might explain the Ku70(-/-)/DNA-PKcs(-/-/-) radioresistance, we monitored HR activities directly in Ku- and DNA-PKcs-deficient cells. The frequency of intrachromosomal HR induced by the I-SceI restriction enzyme was increased in the absence of Ku but not of DNA-PKcs. Significantly, abrogation of HR activity by targeting RAD54 in Ku70(-/-) or DNA-PKcs(-/-/-) cells caused extreme radiosensitivity, suggesting that the relative radioresistance seen with loss of Ku70 was because of HR-dependent repair pathways. Our findings suggest that Ku can interfere with HR-mediated DSB repair, perhaps competing with HR for DSB recognition.

MeSH Terms
Animals Antigens, Nuclear Blotting, Western Cell Cycle Cell Line Chickens Chromatids/physiology DNA/metabolism DNA Damage DNA Helicases DNA Repair DNA-Activated Protein Kinase DNA-Binding Proteins/physiology Dimerization Dose-Response Relationship, Radiation Exons G2 Phase Genotype Ku Autoantigen Mice Nocodazole/pharmacology Nuclear Proteins/physiology Protein Serine-Threonine Kinases/genetics,metabolism Recombination, Genetic S Phase
Chemicals
Antigens, Nuclear DNA-Binding Proteins Nuclear Proteins DNA DNA-Activated Protein Kinase Protein Serine-Threonine Kinases DNA Helicases XRCC5 protein, human Xrcc6 protein, human Xrcc6 protein, mouse Ku Autoantigen Nocodazole
Authors & Affiliations
12 authors, click to expand affiliations / ORCID
Fukushima T
CREST Research Project, Radiation Genetics, Faculty of Medicine, Kyoto University, Konoe Yoshida, Sakyo-ku, Kyoto 606-8501, Japan.
Takata M
Morrison C
Araki R
Fujimori A
Abe M
Tatsumi K
Jasin M
Dhar P K
Sonoda E
Chiba T
Takeda S
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
2001-11-30
Epub
2001-00-27
Pages
44413-8
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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