Detailed Information on Publication Record
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 |
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GA13-26629S, research and development project |
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