Home LiteratureArticle Details
PMID: 15574326 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

A biochemically defined system for mammalian nonhomologous DNA end joining.

Molecular cell ·Vol. 16 ·No. 5 ·2004-12-03 ·Pages 701-13

Ma Y, Lu H, Tippin B, Goodman MF, Shimazaki N, Koiwai O, Hsieh CL, Schwarz K, Lieber MR

Abstract

Nonhomologous end joining (NHEJ) is a major pathway in multicellular eukaryotes for repairing double-strand DNA breaks (DSBs). Here, the NHEJ reactions have been reconstituted in vitro by using purified Ku, DNA-PK(cs), Artemis, and XRCC4:DNA ligase IV proteins to join incompatible ends to yield diverse junctions. Purified DNA polymerase (pol) X family members (pol mu, pol lambda, and TdT, but not pol beta) contribute to junctional additions in ways that are consistent with corresponding data from genetic knockout mice. The pol lambda and pol mu contributions require their BRCT domains and are both physically and functionally dependent on Ku. This indicates a specific biochemical function for Ku in NHEJ at incompatible DNA ends. The XRCC4:DNA ligase IV complex is able to ligate one strand that has only minimal base pairing with the antiparallel strand. This important aspect of the ligation leads to an iterative strand-processing model for the steps of NHEJ.

MeSH Terms
Animals Antigens, Nuclear/metabolism Base Sequence DNA/chemistry,genetics DNA Damage DNA Repair DNA-Activated Protein Kinase DNA-Binding Proteins/metabolism DNA-Directed DNA Polymerase/chemistry,metabolism Endonucleases Escherichia coli/metabolism Ku Autoantigen Models, Biological Models, Genetic Molecular Sequence Data Mutation Nuclear Proteins/metabolism Oligonucleotides/chemistry Protein Binding Protein Serine-Threonine Kinases/metabolism Protein Structure, Tertiary Sequence Homology, Nucleic Acid
Chemicals
Antigens, Nuclear DNA-Binding Proteins Nuclear Proteins Oligonucleotides XRCC4 protein, human DNA DNA-Activated Protein Kinase Protein Serine-Threonine Kinases DNA polymerase X DNA-Directed DNA Polymerase Endonucleases Dclre1c protein, mouse Xrcc6 protein, human Xrcc6 protein, mouse Ku Autoantigen
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Ma Yunmei
University of Southern California Norris Comprehensive Cancer Center, Room 5428, Department of Pathology, University of Southern California Keck School, of Medicine, 1441 Eastlake Avenue, MC9176, Los Angeles, California 90033, USA.
Lu Haihui
Tippin Brigette
Goodman Myron F
Shimazaki Noriko
Koiwai Osamu
Hsieh Chih-Lin
Schwarz Klaus
Lieber Michael R
Article Info
Journal
Molecular cell
Abbr.
Mol Cell
ISSN
1097-2765
Published
2004-12-03
Pages
701-13
Language
English
Region
United States
NLM ID
9802571
Subset
IM
Grants
NCI NIH HHS · CA100504 · United States
NIEHS NIH HHS · ES012259 · United States
NIGMS NIH HHS · GM 43236 · United States
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com