NDLI: Mobile D-loops are a preferred substrate for the Bloom's syndrome helicase

Content Provider	PubMed Central
Author	Bachrati, Csanád Z. Borts, Rhona H. Hickson, Ian D.
Copyright Year	2006
Abstract	The Bloom's syndrome helicase, BLM, is a member of the highly conserved RecQ family, and possesses both DNA unwinding and DNA strand annealing activities. BLM also promotes branch migration of Holliday junctions. One role for BLM is to act in conjunction with topoisomerase IIIα to process homologous recombination (HR) intermediates containing a double Holliday junction by a process termed dissolution. However, several lines of evidence suggest that BLM may also act early in one or more of the recombination pathways to eliminate illegitimate or aberrantly paired DNA joint molecules. We have investigated whether BLM can disrupt DNA displacement loops (D-loops), which represent the initial strand invasion step of HR. We show that mobile D-loops created by the RecA recombinase are a highly preferred substrate for BLM with the invading strand being displaced from the duplex. We have identified structural features of the D-loop that determine the efficiency with which BLM promotes D-loop dissociation. We discuss these results in the context of models for the role of BLM as an ‘anti-recombinase’.
Related Links	http://dx.doi.org/10.1093/nar/gkl258
Ending Page	2279
Page Count	11
Starting Page	2269
File Format	PDF
ISSN	03051048
e-ISSN	13624962
Journal	Nucleic Acids Research
Issue Number	8
Volume Number	34
Language	English
Publisher	Oxford University Press
Publisher Date	2006-04-28
Access Restriction	Open
Rights Holder	Oxford University Press
Subject Keyword	Genetics Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Genetics

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Mobile D-loops are a preferred substrate for the Bloom's syndrome helicase

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Crystal structure of the Bloom's syndrome helicase indicates a role for the HRDC domain in conformational changes

The Bloom's syndrome helicase promotes the annealing of complementary single-stranded DNA

Structural and functional characterizations reveal the importance of a zinc binding domain in Bloom's syndrome helicase

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Complex activities of the human Bloom's syndrome helicase are encoded in a core region comprising the RecA and Zn-binding domains

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