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| pubmed-article:10572166 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:10572166 | pubmed:dateCreated | 2000-1-25 | lld:pubmed |
| pubmed-article:10572166 | pubmed:abstractText | Ku protein and the DNA-dependent protein kinase catalytic subunit (DNA-PKcs) are essential components of the double-strand break repair machinery in higher eukaryotic cells. Ku protein binds to broken DNA ends and recruits DNA-PKcs to form an enzymatically active complex. To characterize the arrangement of proteins in this complex, we developed a set of photocross-linking probes, each with a single free end. We have previously used this approach to characterize the contacts in an initial Ku-DNA complex, and we have now applied the same technology to define the events that occur when Ku recruits DNA-PKcs. The new probes allow the binding of one molecule of Ku protein and one molecule of DNA-PKcs in a defined position and orientation. Photocross-linking reveals that DNA-PKcs makes direct contact with the DNA termini, occupying an approximately 10 bp region proximal to the free end. Characterization of the Ku protein cross-linking pattern in the presence and absence of DNA-PKcs suggests that Ku binds to form an initial complex at the DNA ends, and that recruitment of DNA-PKcs induces an inward translocation of this Ku molecule by about one helical turn. The presence of ATP had no effect on protein-DNA contacts, suggesting that neither DNA-PK-mediated phosphorylation nor a putative Ku helicase activity plays a role in modulating protein conformation under the conditions tested. | lld:pubmed |
| pubmed-article:10572166 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:10572166 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10572166 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10572166 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:10572166 | pubmed:issn | 1362-4962 | lld:pubmed |
| pubmed-article:10572166 | pubmed:author | pubmed-author:DynanW SWS | lld:pubmed |
| pubmed-article:10572166 | pubmed:author | pubmed-author:YooSS | lld:pubmed |
| pubmed-article:10572166 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:10572166 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:10572166 | pubmed:volume | 27 | lld:pubmed |
| pubmed-article:10572166 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10572166 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10572166 | pubmed:pagination | 4679-86 | lld:pubmed |
| pubmed-article:10572166 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:10572166 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10572166 | pubmed:articleTitle | Geometry of a complex formed by double strand break repair proteins at a single DNA end: recruitment of DNA-PKcs induces inward translocation of Ku protein. | lld:pubmed |
| pubmed-article:10572166 | pubmed:affiliation | Program in Gene Regulation, Institute of Molecular Medicine and Genetics, Medical College of Georgia, 1120 15th Street, Augusta, GA 30912, USA. | lld:pubmed |
| pubmed-article:10572166 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10572166 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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