Reduced repair of DNA double-strand breaks by homologous recombination in a DNA ligase I-deficient human cell line Journal Article

  

Authors:	Goetz, J. D. M.; Motycka, T. A.; Han, M.; Jasin, M.; Tomkinson, A. E.
Article Title:	Reduced repair of DNA double-strand breaks by homologous recombination in a DNA ligase I-deficient human cell line
Abstract:	Genetic and biochemical studies of mammalian DNA ligase I indicate that this multifunctional enzyme plays a key role in the completion of DNA replication and certain DNA excision repair pathways. However, the involvement of DNA ligase I in DNA double-strand break repair has not been examined. Here we have determined the effect of DNA ligase I-deficiency on the frequency of homologous recombination initiated by a site-specific DNA double-strand break. We found that expression of wild-type DNA ligase I in a human DNA ligase I mutant cell line significantly increased the frequency of homologous recombination. Notably, the ability of DNA ligase I to promote the recombinational repair of DNA double-strand breaks was dependent upon its interaction with proliferating cell nuclear antigen. Thus, our results demonstrate that DNA ligase I-deficiency reduces recombinational repair of DNA double-strand breaks. © 2005 Elsevier B.V. All rights reserved.
Keywords:	controlled study; unclassified drug; nonhuman; genetic analysis; protein function; mammalia; dna damage; homologous recombination; dna repair; protein protein interaction; cell line; wild type; dna strand breakage; double stranded dna; enzyme analysis; recombination, genetic; dna double-strand break repair; cycline; polydeoxyribonucleotide synthase; cell mutant; dna ligases; proliferating cell nuclear antigen; pcna; dna ligase i; polydeoxyribonucleotide synthase 1
Journal Title:	DNA Repair
Volume:	4
Issue:	6
ISSN:	1568-7864
Publisher:	Elsevier Inc.
Date Published:	2005-06-08
Start Page:	649
End Page:	654
Language:	English
DOI:	10.1016/j.dnarep.2005.02.004
PUBMED:	15907772
PROVIDER:	scopus
DOI/URL:	http://www.scopus.com/inward/record.url?eid=2-s2.0-19344366421&partnerID=40&md5=ccb8d903edd1673720b308608cd71191
Notes:	--- - "Cited By (since 1996): 11" - "Export Date: 24 October 2012" - "CODEN: DRNEA" - "Source: Scopus"

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