Sumoylation of RecQ helicase controls the fate of dysfunctional telomeres.

Rog O; Miller KM; Ferreira MG; Cooper JP

doi:10.1016/j.molcel.2009.01.027

Sumoylation of RecQ helicase controls the fate of dysfunctional telomeres.

ARTICLE PUBLISHED: 2009 Mar 13

CITE AS: Mol Cell. 2009 Mar 13; 33(5):559-569 https://doi.org/10.1016/j.molcel.2009.01.027

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Genome stability depends upon the RecQ helicases, which are conserved from bacteria to man, but little is known about how their myriad activities are regulated. Fission yeast lacking the telomere protein Taz1 (mammalian TRF1/TRF2 ortholog) lose many hallmarks of telomeres, including accurate replication and local protection from DNA repair reactions. Here we show that the RecQ homolog, Rqh1, is sumoylated. Surprisingly, Rqh1 acts on taz1Delta telomeres in a deleterious way, promoting telomere breakage and entanglement. Mutation of Rqh1 sumoylation sites rescues taz1Delta cells from these hazards without dramatically affecting nontelomeric Rqh1 functions. The prominence of Rqh1 in the etiology of several different telomere defects supports the idea that they originate from a common underlying lesion--aberrant processing of the stalled telomeric replication forks that accumulate in the absence of Taz1. Our work underscores the principle that RecQ helicases are "double-edged swords" whose activity, while necessary for maintaining genome-wide stability, must be vigilantly controlled.

PMID: 19285940
Funding information

This work was supported by:
- Cancer Research UK, United Kingdom
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Relevant Sections

Cell Biology
- Cell Growth & Division
- Nuclear Structure & Function
Microbiology
- Microbial Growth & Development
Structural Biology
- Structure: Replication, Recombination & Repair

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Sumoylation of RecQ helicase controls the fate of dysfunctional telomeres.

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Cancer Research UK, United Kingdom

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