Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Editorial
. 2010 Aug 15;9(16):3139-41.
doi: 10.4161/cc.9.16.12953. Epub 2010 Aug 9.

Genetic mutants illuminate the roles of RecQ helicases in recombinational repair or response to replicational stress

Monika Aggarwal, Robert M Brosh Jr
Editorial

Genetic mutants illuminate the roles of RecQ helicases in recombinational repair or response to replicational stress

Monika Aggarwal et al. Cell Cycle. .
No abstract available

PubMed Disclaimer

Figures

Figure 1
Figure 1
Model for the roles of BLM and WRN helicases in collaboration with EXO1 to process DNA double strand breaks or structures associated with stalled replication forks. (A) BLM stimulates the EXO1 nucleolytic processing at direct DSB ends. EXO1 resects DNA ends, albeit with reduced efficiency to generate short ssDNA tails. BLM interacts with EXO1 and enhances its processivity to generate long 3′ ssDNA tailed molecules that can be used for the strand invasion step of HR repair. (B) WRN collaborates with EXO1 to prevent deleterious events at DNA replication forks impeded by alkylated base damage. I. EXO1 nucleolytic activity at the newly synthesized lagging strand of a stalled replication fork is limited. WRN interacts with EXO1 and stimulates 5′ incision of the lagging strand arm thus resolving the sister chromatid junction to prevent reversal at the collapsed replication fork. II. After fork regression has taken place, EXO1 resection of the free 5′ end of the Holliday Junction-like structure is limited. WRN stimulates EXO1 nucleolytic activity to generate a three-stranded structure that can be stabilized by a Rad51-like protein while the lesion is being repaired.
See this image and copyright information in PMC

Similar articles

See all similar articles

Cited by

References

    1. Lisby M, et al. DNA Repair (Amst) 2009;8:1068–76. - PMC - PubMed
    1. Mimitou EP, et al. Trends Biochem Sci. 2009;34:264–72. - PubMed
    1. Brosh RM, Jr, et al. Nucleic Acids Res. 2007;35:7527–44. - PMC - PubMed
    1. Rossi ML, et al. DNA Repair (Amst) 2010;9:331–44. - PMC - PubMed
    1. Sharma S, et al. Hum Mol Genet. 2004;13:2247–61. - PubMed

Publication types

LinkOut - more resources