J 2012

Dual roles of the SUMO-interacting motif in the regulation of Srs2 sumoylation.

KOLESÁR, Peter, Prabha SARANGI, Veronika ALTMANNOVÁ, Xiaolan ZHAO, Lumír KREJČÍ et. al.

Basic information

Original name

Dual roles of the SUMO-interacting motif in the regulation of Srs2 sumoylation.

Authors

KOLESÁR, Peter (703 Slovakia, belonging to the institution), Prabha SARANGI (356 India), Veronika ALTMANNOVÁ (203 Czech Republic, belonging to the institution), Xiaolan ZHAO (840 United States of America) and Lumír KREJČÍ (203 Czech Republic, guarantor, belonging to the institution)

Edition

Nucleic Acids Research, Oxford, Oxford University Press, 2012, 0305-1048

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

Czech Republic

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

Impact factor

Impact factor: 8.278

RIV identification code

RIV/00216224:14110/12:00057621

Organization unit

Faculty of Medicine

DOI

UT WoS

000308959800028

Keywords in English

Srs2 SUMO PCNA
Změněno: 22/4/2013 16:19, Soňa Böhmová

Abstract

V originále

The Srs2 DNA helicase of Saccharomyces cerevisiae affects recombination in multiple ways. Srs2 not only inhibits recombination at stalled replication forks but also promotes the synthesis-dependent strand annealing (SDSA) pathway of recombination. Both functions of Srs2 are regulated by sumoylation-sumoylated PCNA recruits Srs2 to the replication fork to disfavor recombination, and sumoylation of Srs2 can be inhibitory to SDSA in certain backgrounds. To understand Srs2 function, we characterize the mechanism of its sumoylation in vitro and in vivo. Our data show that Srs2 is sumoylated at three lysines, and its sumoylation is facilitated by the Siz SUMO ligases. We also show that Srs2 binds to SUMO via a C-terminal SUMO-interacting motif (SIM). The SIM region is required for Srs2 sumoylation, likely by binding to SUMO-charged Ubc9. Srs2's SIM also cooperates with an adjacent PCNA-specific interaction site in binding to sumoylated PCNA to ensure the specificity of the interaction. These two functions of Srs2's SIM exhibit a competitive relationship: sumoylation of Srs2 decreases the interaction between the SIM and SUMO-PCNA, and the SUMO-PCNA-SIM interaction disfavors Srs2 sumoylation. Our findings suggest a potential mechanism for the equilibrium of sumoylated and PCNA-bound pools of Srs2 in cells.

Links

EE2.3.09.0186, research and development project
Name: Mendelovo centrum pro vzdělávání v biologii, biomedicíně a bioinformatice
GAP207/12/2323, research and development project
Name: Endonuleazová a translokázová aktivita v restričních-modifikáčních komplexéch typu I
Investor: Czech Science Foundation
GA301/09/1917, research and development project
Name: Štěpení replikačních-rekombinačních DNA meziproduktů a jejich úloha při nestabilitě genomu
Investor: Czech Science Foundation
GD203/09/H046, research and development project
Name: Biochemie na rozcestí mezi in silico a in vitro
Investor: Czech Science Foundation
LC06030, research and development project
Name: Biomolekulární centrum
Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular centre
ME10048, research and development project
Name: Vliv post-translačních modifikací na DNA opravu a rekombinaci.
Investor: Ministry of Education, Youth and Sports of the CR, Research and Development Programme KONTAKT (ME)
MSM0021622413, plan (intention)
Name: Proteiny v metabolismu a při interakci organismů s prostředím
Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment
MUNI/A/0822/2011, interní kód MU
Name: Molekulární a buněčná biologie v biomedicíně
Investor: Masaryk University, Category A