pubmed-article:18250087 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18250087 | lifeskim:mentions | umls-concept:C0019644 | lld:lifeskim |
pubmed-article:18250087 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
pubmed-article:18250087 | lifeskim:mentions | umls-concept:C1518406 | lld:lifeskim |
pubmed-article:18250087 | lifeskim:mentions | umls-concept:C1704259 | lld:lifeskim |
pubmed-article:18250087 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
pubmed-article:18250087 | lifeskim:mentions | umls-concept:C1705987 | lld:lifeskim |
pubmed-article:18250087 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:18250087 | pubmed:dateCreated | 2008-3-17 | lld:pubmed |
pubmed-article:18250087 | pubmed:abstractText | DNA double-strand breaks (DSBs) induced in the genome of higher eukaryotes by ionizing radiation (IR) are predominantly removed by two pathways of non-homologous end-joining (NHEJ) termed D-NHEJ and B-NHEJ. While D-NHEJ depends on the activities of the DNA-dependent protein kinase (DNA-PK) and DNA ligase IV/XRCC4/XLF, B-NHEJ utilizes, at least partly, DNA ligase III/XRCC1 and PARP-1. Using in vitro end-joining assays and protein fractionation protocols similar to those previously applied for the characterization of DNA ligase III as an end-joining factor, we identify here histone H1 as an additional putative NHEJ factor. H1 strongly enhances DNA-end joining and shifts the product spectrum from circles to multimers. While H1 enhances the DNA-end-joining activities of both DNA Ligase IV and DNA Ligase III, the effect on ligase III is significantly stronger. Histone H1 also enhances the activity of PARP-1. Since histone H1 has been shown to counteract D-NHEJ, these observations and the known functions of the protein identify it as a putative alignment factor operating preferentially within B-NHEJ. | lld:pubmed |
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pubmed-article:18250087 | pubmed:language | eng | lld:pubmed |
pubmed-article:18250087 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18250087 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:18250087 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18250087 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18250087 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18250087 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18250087 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:18250087 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18250087 | pubmed:month | Mar | lld:pubmed |
pubmed-article:18250087 | pubmed:issn | 1362-4962 | lld:pubmed |
pubmed-article:18250087 | pubmed:author | pubmed-author:IliakisGeorge... | lld:pubmed |
pubmed-article:18250087 | pubmed:author | pubmed-author:WangMinliM | lld:pubmed |
pubmed-article:18250087 | pubmed:author | pubmed-author:SharmaAparnaA | lld:pubmed |
pubmed-article:18250087 | pubmed:author | pubmed-author:WangHuichenH | lld:pubmed |
pubmed-article:18250087 | pubmed:author | pubmed-author:RosidiBustanu... | lld:pubmed |