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Papers In Press, published online ahead of print April 4, 2006
Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06520
Corresponding Author: patrick.sung{at}yale.edu
Bloom’s syndrome (BS), an autosomal recessive disorder, is marked by a high incidence of cancer early in life. Cells derived from BS patients are unstable genetically and exhibit frequent sister chromatid exchanges, reflective of homologous recombination (HR) deregulation. BLM, the RecQ-like helicase mutated in BS, is found in several cellular protein complexes, all of which contain topoisomerase IIIa (Topo IIIa) and a novel protein BLAP75. Here, using highly purified human proteins, we show that BLAP75 associates independently with both Topo IIIa and BLM. Even though BLM and Topo IIIa can dissolve the double Holliday junction (DHJ) to yield non-crossover recombinants, under physiological conditions, DHJ dissolution becomes completely dependent on BLAP75. The effect of BLAP75 on BLM-Topo IIIa is highly specific, as it is not seen with the combination of Topo IIIa and E. coli RecQ helicase or another human RecQ-like helicase WRN. Thus, BLM, Topo IIIa, and BLAP75 constitute a dissolvasome complex that processes HR intermediates to limit DNA crossover formation. This function of the BLM-Topo IIIa-BLAP75 dissolvasome is likely indispensable for genome maintenance and cancer avoidance.
J. Biol. Chem, 10.1074/jbc.C600051200
Submitted on March 3, 2006
Revised on March 29, 2006
Accepted on March 31, 2006
A double holliday junction dissolvasome comprising BLM, topoisomerase III
, and BLAP75
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