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- Title
Aggregative organization enhances the DNA end-joining process that is mediated by DNA-dependent protein kinase.
- Authors
Takahagi, Masahiko; Tatsumi, Kouichi
- Abstract
The occurrence of DNA double-strand breaks in the nucleus provokes in its structural organization a large-scale alteration whose molecular basis is still mostly unclear. Here, we show that double-strand breaks trigger preferential assembly of nucleoproteins in human cellular fractions and that they mediate the separation of large protein–DNA aggregates from aqueous solution. The interaction among the aggregative nucleoproteins presents a dynamic condition that allows the effective interaction of nucleoproteins with external molecules like free ATP and facilitates intrinsic DNA end-joining activity. This aggregative organization is functionally coacervate-like. The key component is DNA-dependent protein kinase (DNA-PK), which can be characterized as a DNA-specific aggregation factor as well as a nuclear scaffold/matrix-interactive factor. In the context of aggregation, the kinase activity of DNA-PK is essential for efficient DNA end-joining. The massive and functional concentration of nucleoproteins on DNA in vitro may represent a possible status of nuclear dynamics in vivo, which probably includes the DNA-PK-dependent response to multiple double-strand breaks.
- Subjects
DNA; PROTEIN kinases; NUCLEOPROTEINS; CYTOLOGY; MOLECULAR biology
- Publication
FEBS Journal, 2006, Vol 273, Issue 13, p3063
- ISSN
1742-464X
- Publication type
Article
- DOI
10.1111/j.1742-4658.2006.05317.x