J 2013

Lif1 SUMOylation and its role in non-homologous end-joining

VIGAŠOVÁ, Dana, Prabha SARANGI, Peter KOLESÁR, Danusa VLASAKOVA, Zuzana SLEZÁKOVÁ et. al.

Basic information

Original name

Lif1 SUMOylation and its role in non-homologous end-joining

Authors

VIGAŠOVÁ, Dana (703 Slovakia, belonging to the institution), Prabha SARANGI (840 United States of America), Peter KOLESÁR (703 Slovakia, belonging to the institution), Danusa VLASAKOVA (703 Slovakia), Zuzana SLEZÁKOVÁ (703 Slovakia, belonging to the institution), Veronika ALTMANNOVÁ (203 Czech Republic, belonging to the institution), Fedor NIKULENKOV (643 Russian Federation, belonging to the institution), Dorothea ANRATHER (40 Austria), Rainer GITH (840 United States of America), Xiaolan ZHAO (840 United States of America), Miroslav CHOVANEC (703 Slovakia) and Lumír KREJČÍ (203 Czech Republic, guarantor, belonging to the institution)

Edition

Nucleic Acids Research, Oxford, Oxford Press, 2013, 0305-1048

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

United Kingdom of Great Britain and Northern Ireland

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

Impact factor

Impact factor: 8.808

RIV identification code

RIV/00216224:14110/13:00066405

Organization unit

Faculty of Medicine

UT WoS

000319806600024

Keywords in English

DOUBLE-STRAND BREAKS; DNA-LIGASE-IV; SACCHAROMYCES-CEREVISIAE; CRYSTAL-STRUCTURE; FUNCTIONAL INTERACTION; REPAIR PATHWAY; YEAST SEPTINS/; MATING-TYPE; PROTEIN; SUMO

Tags

Tags

International impact, Reviewed
Změněno: 28/4/2014 17:40, Ing. Mgr. Věra Pospíšilíková

Abstract

V originále

Non-homologous end-joining (NHEJ) repairs DNA double-strand breaks by tethering and ligating the two DNA ends. The mechanisms regulating NHEJ efficiency and interplay between its components are not fully understood. Here, we identify and characterize the SUMOylation of budding yeast Lif1 protein, which is required for the ligation step in NHEJ. We show that Lif1 SUMOylation occurs throughout the cell cycle and requires the Siz SUMO ligases. Single-strand DNA, but not double-strand DNA or the Lif1 binding partner Nej1, is inhibitory to Lif1 SUMOylation. We identify lysine 301 as the major conjugation site and demonstrate that its replacement with arginine completely abolishes Lif1 SUMOylation in vivo and in vitro. The lif1-K301R mutant cells exhibit increased levels of NHEJ repair compared with wild-type cells throughout the cell cycle. This is likely due to the inhibitory effect of Lif1 SUMOylation on both its self-association and newly observed single-strand DNA binding activity. Taken together, these findings suggest that SUMOylation of Lif1 represents a new regulatory mechanism that downregulates NHEJ in a cell cycle phase-independent manner.

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