J 2015

Srs2 promotes Mus81-Mms4-mediated resolution of recombination intermediates

CHAVDAROVA, Melita, María Victoria MARINI PALOMEQUE, Alexandra SISÁKOVÁ, Hana SEDLÁČKOVÁ, Dana VIGAŠOVÁ et. al.

Basic information

Original name

Srs2 promotes Mus81-Mms4-mediated resolution of recombination intermediates

Authors

CHAVDAROVA, Melita (807 North Macedonia, belonging to the institution), María Victoria MARINI PALOMEQUE (858 Uruguay, belonging to the institution), Alexandra SISÁKOVÁ (703 Slovakia, belonging to the institution), Hana SEDLÁČKOVÁ (203 Czech Republic, belonging to the institution), Dana VIGAŠOVÁ (703 Slovakia, belonging to the institution), Steven J. BRILL (840 United States of America), Michael LISBY (208 Denmark) and Lumír KREJČÍ (203 Czech Republic, guarantor, belonging to the institution)

Edition

Nucleic Acids Research, Oxford, Oxford Press, 2015, 0305-1048

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

Genetics and molecular biology

Country of publisher

United Kingdom of Great Britain and Northern Ireland

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 9.202

RIV identification code

RIV/00216224:14110/15:00080935

Organization unit

Faculty of Medicine

UT WoS

000354722500025

Keywords in English

SACCHAROMYCES-CEREVISIAE SRS2; POSTREPLICATION REPAIR PATHWAY; RAD51 PRESYNAPTIC FILAMENT; DOUBLE-STRAND BREAKS; HOMOLOGOUS RECOMBINATION; DNA HELICASE; REPLICATION FORKS; FISSION YEAST; MITOTIC RECOMBINATION; CELL-CYCLE

Tags

Tags

International impact, Reviewed
Změněno: 29/7/2015 12:36, Ing. Mgr. Věra Pospíšilíková

Abstract

V originále

A variety of DNA lesions, secondary DNA structures or topological stress within the DNA template may lead to stalling of the replication fork. Recovery of such forks is essential for the maintenance of genomic stability. The structure-specific endonuclease Mus81-Mms4 has been implicated in processing DNA intermediates that arise from collapsed forks and homologous recombination. According to previous genetic studies, the Srs2 helicase may play a role in the repair of double-strand breaks and ssDNA gaps together with Mus81-Mms4. In this study, we show that the Srs2 and Mus81-Mms4 proteins physically interact in vitro and in vivo and we map the interaction domains within the Srs2 and Mus81 proteins. Further, we show that Srs2 plays a dual role in the stimulation of the Mus81-Mms4 nuclease activity on a variety of DNA substrates. First, Srs2 directly stimulates Mus81-Mms4 nuclease activity independent of its helicase activity. Second, Srs2 removes Rad51 from DNA to allow access of Mus81-Mms4 to cleave DNA. Concomitantly, Mus81-Mms4 inhibits the helicase activity of Srs2. Taken together, our data point to a coordinated role of Mus81-Mms4 and Srs2 in processing of recombination as well as replication intermediates.

Links

GAP207/12/2323, research and development project
Name: Endonuleazová a translokázová aktivita v restričních-modifikáčních komplexéch typu I
Investor: Czech Science Foundation
GA13-26629S, research and development project
Name: SUMO a stability genomu
Investor: Czech Science Foundation