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Replication protein A physically interacts with the Bloom's syndrome protein and stimulates its helicase activity.

Authors: Brosh RM, JR  Li, JL  Kenny, MK  Karow, JK  Cooper, MP  Kureekattil, RP  Hickson, ID  Bohr, VA 
Citation: Brosh RM Jr, etal., J Biol Chem. 2000 Aug 4;275(31):23500-8.
Pubmed: (View Article at PubMed) PMID:10825162
DOI: Full-text: DOI:10.1074/jbc.M001557200

Bloom's syndrome is a rare autosomal recessive disorder characterized by genomic instability and predisposition to cancer. BLM, the gene defective in Bloom's syndrome, encodes a 159-kDa protein possessing DNA-stimulated ATPase and ATP-dependent DNA helicase activities. We have examined mechanistic aspects of the catalytic functions of purified recombinant BLM protein. Through analyzing the effects of different lengths of DNA cofactor on ATPase activity, we provide evidence to suggest that BLM translocates along single-stranded DNA in a processive manner. The helicase reaction catalyzed by BLM protein was examined as a function of duplex DNA length. We show that BLM catalyzes unwinding of short DNA duplexes (/=259-bp). The presence of the human single-stranded DNA-binding protein (human replication protein A (hRPA)) stimulates the BLM unwinding reaction on the 259-bp partial duplex DNA substrate. Heterologous single-stranded DNA-binding proteins fail to stimulate similarly the helicase activity of BLM protein. This is the first demonstration of a functional interaction between BLM and another protein. Consistent with a functional interaction between hRPA and the BLM helicase, we demonstrate a direct physical interaction between the two proteins mediated by the 70-kDa subunit of RPA. The interactions between BLM and hRPA suggest that the two proteins function together in vivo to unwind DNA duplexes during replication, recombination, or repair.

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CRRD Object Information
CRRD ID: 1580057
Created: 2006-06-21
Species: All species
Last Modified: 2006-06-21
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.