DUNO, Morten, Bo THOMSEN, Ole WESTERGAARD, Lumír KREJČÍ and Christian BENDIXEN. Genetic analysis of the Saccharomyces cerevisiae Sgs1 helicase defines an essential function for the Sgs1-Top3 complex in the absence of SRS2 or TOP1. Mol Gen Genet. 2000, vol. 264, 1-2, p. 89-97, 8 pp. ISSN 1617-4615.
Other formats:   BibTeX LaTeX RIS
Basic information
Original name Genetic analysis of the Saccharomyces cerevisiae Sgs1 helicase defines an essential function for the Sgs1-Top3 complex in the absence of SRS2 or TOP1.
Name in Czech Genetic analysis of the Saccharomyces cerevisiae Sgs1 helicase defines an essential function for the Sgs1-Top3 complex in the absence of SRS2 or TOP1.
Authors DUNO, Morten (208 Denmark), Bo THOMSEN (208 Denmark), Ole WESTERGAARD (208 Denmark), Lumír KREJČÍ (203 Czech Republic, guarantor) and Christian BENDIXEN (208 Denmark).
Edition Mol Gen Genet, 2000, 1617-4615.
Other information
Original language English
Type of outcome Article in a journal
Field of Study Genetics and molecular biology
Country of publisher Denmark
Confidentiality degree is not subject to a state or trade secret
Organization unit Faculty of Science
Keywords in English Recombination; repair; Sgs1;Top3
Tags recombination, repair, Sgs1, Top3
Tags International impact, Reviewed
Changed by Changed by: doc. Mgr. Lumír Krejčí, Ph.D., učo 18098. Changed: 15/5/2009 23:04.
Abstract
The Saccharomyces cerevisiae gene SGS1 encodes a DNA helicase that shows homology to the Escherichia coli protein RecQ and the products of the BLM and WRN genes in humans, which are defective in Bloom's and Werner's syndrome, respectively. Recently, it has been proposed that this helicase is involved in maintaining the integrity of the rDNA and that loss of Sgs1 function leads to accelerated aging. Sgs1 has been isolated on the basis of its genetic interaction with both topoisomerase I and topoisomerase III, as well as in a two-hybrid screen for proteins that interact with the C-terminal portion of topoisomerase II. We have defined the minimal structural elements of Sgs1 required for its interactions with the three topoisomerases, and demonstrate that the complex phenotypes associated with sgs1 mutants are a consequence of a dysfunctional Sgs1-Top3 complex. We also report that the synthetic relationship between mutations in SGS1 and SRS2, which encodes another helicase implicated in recombinational repair, likewise result from a dysfunctional Sgs1-Top3 interaction. Our findings indicate that Sgs1 may act on different DNA structures depending on the activity of topoisomerase I, Srs2 and topoisomerase III.
Abstract (in Czech)
Genetická charakterizace SGS1 a TOP1 vztahů
PrintDisplayed: 18/8/2024 08:20