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PMID: 10377944 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Ku, a DNA repair protein with multiple cellular functions?

Mutation research ·Vol. 434 ·No. 1 ·1999-05-14 ·Pages 3-15

Featherstone C, Jackson SP

Abstract

The Ku protein binds to DNA ends and other types of discontinuity in double-stranded DNA. It is a tightly associated heterodimer of approximately 70 kDa and approximately 80 kDa subunits that together with the approximately 470 kDa catalytic subunit, DNA-PKcs, form the DNA-dependent protein kinase. This enzyme is involved in repairing DNA double-strand breaks (DSBs) caused, for example, by physiological oxidation reactions, V(D)J recombination, ionizing radiation and certain chemotherapeutic drugs. The Ku-dependent repair process, called illegitimate recombination or nonhomologous end joining (NHEJ), appears to be the main DNA DSB repair mechanism in mammalian cells. Ku itself is probably involved in stabilizing broken DNA ends, bringing them together and preparing them for ligation. Ku also recruits DNA-PKcs to the DSB, activating its kinase function. Targeted disruption of the genes encoding Ku70 and Ku80 has identified significant differences between Ku-deficient mice and DNA-PKcs-deficient mice. Although all three gene products are clearly involved in repairing ionizing radiation-induced damage and in V(D)J recombination, Ku-knockout mice are small, and their cells fail to proliferate in culture and show signs of premature senescence. Recent findings have implicated yeast Ku in telomeric structure in addition to NHEJ. Some of the phenotypes of the Ku-knockout mice may indicate a similar role for Ku at mammalian telomeres.

MeSH Terms
Animals Antigens, Nuclear DNA Helicases DNA Repair/physiology DNA-Activated Protein Kinase DNA-Binding Proteins/physiology Humans Ku Autoantigen Nuclear Proteins/physiology Protein Serine-Threonine Kinases/physiology Saccharomyces cerevisiae Proteins Telomere/metabolism Transcription, Genetic
Chemicals
Antigens, Nuclear DNA-Binding Proteins Nuclear Proteins Saccharomyces cerevisiae Proteins high affinity DNA-binding factor, S cerevisiae DNA-Activated Protein Kinase PRKDC protein, human Protein Serine-Threonine Kinases DNA Helicases XRCC5 protein, human Xrcc6 protein, human Xrcc6 protein, mouse Ku Autoantigen
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Featherstone C
Wellcome/Cancer Research Campaign Institute, Cambridge University, UK. cf214@mole.bio.cam.ac.uk
Jackson S P
Article Info
Journal
Mutation research
Abbr.
Mutat Res
ISSN
0027-5107
Published
1999-05-14
Pages
3-15
Language
English
Region
Netherlands
NLM ID
0400763
Subset
IM
Grants
Wellcome Trust · United Kingdom
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