Authors: | Suski, C.; Marians, K. J. |
Article Title: | Resolution of converging replication forks by RecQ and topoisomerase III |
Abstract: | RecQ-like DNA helicases pair with cognate topoisomerase III enzymes to function in the maintenance of genomic integrity in many organisms. These proteins play roles in stabilizing stalled replication forks, the S phase checkpoint response, and suppressing genetic crossovers, and their inactivation results in hyperrecombination, gross chromosomal rearrangements, chromosome segregation defects, and human disease. Biochemical activities associated with these enzymes include the ability to resolve double Holliday junctions, a process thought to lead to the suppression of crossover formation. Using Escherichia coli RecQ and topoisomerase III, we demonstrate a second activity for this pair of enzymes that could account for their role in maintaining genomic stability: resolution of converging replication forks. This resolution reaction is specific for the RecQ-topoisomerase III pair and is mediated by interaction of both of these enzymes with the single-stranded DNA-binding protein SSB. © 2008 Elsevier Inc. All rights reserved. |
Keywords: | dna binding protein; nonhuman; dna replication; cell cycle s phase; enzyme activity; dna; genetic recombination; kinetics; genomic instability; escherichia coli; gene repression; chromosome rearrangement; models, molecular; gene inactivation; recq helicases; single stranded dna; nucleic acid conformation; dna, bacterial; s phase; chromosome segregation; escherichia coli proteins; dna topoisomerase; dna topoisomerases, type i; crossing over; molecular stability; recq helicase; dna topoisomerase iii; dna replication timing; genome, bacterial |
Journal Title: | Molecular Cell |
Volume: | 30 |
Issue: | 6 |
ISSN: | 1097-2765 |
Publisher: | Cell Press |
Date Published: | 2008-06-20 |
Start Page: | 779 |
End Page: | 789 |
Language: | English |
DOI: | 10.1016/j.molcel.2008.04.020 |
PUBMED: | 18570879 |
PROVIDER: | scopus |
PMCID: | PMC2459239 |
DOI/URL: | |
Notes: | --- - "Cited By (since 1996): 23" - "Export Date: 17 November 2011" - "CODEN: MOCEF" - "Source: Scopus" |