@article{oai:repo.qst.go.jp:00044669,
 author = {Takahagi, Masahiko and Tatsumi, Kouichi and 高萩 真彦 and 巽 紘一},
 issue = {13},
 journal = {The FEBS Journal},
 month = {Jul},
 note = {The occurrence of DNA double strand breaks (DSBs) in the nucleus provokes in
its structural organization a large-scale alteration whose molecular basis
is still mostly unclear.  Here, we show that DSBs 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 DSBs.},
 pages = {3063--3075},
 title = {Aggregative organization enhances the DNA end-joining process that is mediated by DNA-dependent protein kinase},
 volume = {273},
 year = {2006}
}