Format

Send to:

Choose Destination
See comment in PubMed Commons below
Biophys Chem. 2010 Jul;149(3):67-77. doi: 10.1016/j.bpc.2010.03.012. Epub 2010 Mar 20.

Probing the structural basis of RecQ helicase function.

Author information

  • 1International Centre for Genetic Engineering and Biotechnology, 34149 Trieste, Italy. vindigni@icgeb.org

Abstract

RecQ helicases are a ubiquitous family of DNA unwinding enzymes required to preserve genome integrity, thus preventing premature aging and cancer formation. The five human representatives of this family play non-redundant roles in the suppression of genome instability using a combination of enzymatic activities that specifically characterize each member of the family. These enzymes are in fact not only able to catalyze the transient opening of DNA duplexes, as any other conventional helicase, but can also promote annealing of complementary strands, branch migration of Holliday junctions and, in some cases, excision of ssDNA tails. Remarkably, the balance between these different activities seems to be regulated by protein oligomerization. This review illustrates the recent progress made in the definition of the structural determinants that control the different enzymatic activities of RecQ helicases and speculates on the possible mechanisms that RecQ proteins might use to promote their multiple functions.

Copyright 2010 Elsevier B.V. All rights reserved.

PMID:
20392558
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Write to the Help Desk