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J. Biol. Chem., Vol. 276, Issue 22, 19375-19381, June 1, 2001
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,
From the Imperial Cancer Research Fund Laboratories, Weatherall
Institute of Molecular Medicine, University of Oxford, John Radcliffe
Hospital, Oxford OX3 9DS, United Kingdom
Bloom's syndrome (BS) is an autosomal recessive
disorder that predisposes individuals to a wide range of cancers. The
gene mutated in BS, BLM, encodes a member of the RecQ
family of DNA helicases. The precise role played by these enzymes in
the cell remains to be determined. However, genome-wide
hyper-recombination is a feature of many RecQ helicase-deficient cells.
In eukaryotes, a central step in homologous recombination is catalyzed
by the RAD51 protein. In response to agents that induce DNA
double-strand breaks, RAD51 accumulates in nuclear foci that are
thought to correspond to sites of recombinational repair. Here, we
report that purified BLM and human RAD51 interact in vitro
and in vivo, and that residues in the N- and C-terminal
domains of BLM can independently mediate this interaction. Consistent
with these observations, BLM localizes to a subset of RAD51 nuclear
foci in normal human cells. Moreover, the number of BLM foci and the extent to which BLM and RAD51 foci co-localize increase in response to
ionizing radiation. Nevertheless, the formation of RAD51 foci does not
require functional BLM. Indeed, in untreated BS cells, an abnormally
high proportion of the cells contain RAD51 nuclear foci. Exogenous
expression of BLM markedly reduces the fraction of cells containing
RAD51 foci. The interaction between BLM and RAD51 appears to have been
evolutionarily conserved since the C-terminal domain of Sgs1, the
Saccharomyces cerevisiae homologue of BLM, interacts with
yeast Rad51. Furthermore, genetic analysis reveals that the
SGS1 and RAD51 genes are epistatic indicating that they operate in a common pathway. Potential roles for BLM in the
RAD51 recombinational repair pathway are discussed.
To whom correspondence should be addressed. Tel.: 44-1865-222427;
Fax: 44-1865-222431; E-mail: wu@icrf.icnet.uk.
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