VIGAŠOVÁ, Dana, Prabha SARANGI, Peter KOLESÁR, Danusa VLASAKOVA, Zuzana SLEZÁKOVÁ, Veronika ALTMANNOVÁ, Fedor NIKULENKOV, Dorothea ANRATHER, Rainer GITH, Xiaolan ZHAO, Miroslav CHOVANEC and Lumír KREJČÍ. Lif1 SUMOylation and its role in non-homologous end-joining. Nucleic Acids Research. Oxford: Oxford Press, 2013, vol. 41, No 10, p. 5341-5353. ISSN 0305-1048. Available from: https://dx.doi.org/10.1093/nar/gkt236.
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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
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher United Kingdom of Great Britain and Northern Ireland
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 8.808
RIV identification code RIV/00216224:14110/13:00066405
Organization unit Faculty of Medicine
Doi http://dx.doi.org/10.1093/nar/gkt236
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 podil
Tags International impact, Reviewed
Changed by Changed by: Ing. Mgr. Věra Pospíšilíková, učo 9005. Changed: 28/4/2014 17:40.
Abstract
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 projectName: Endonuleazová a translokázová aktivita v restričních-modifikáčních komplexéch typu I
Investor: Czech Science Foundation
GA13-26629S, research and development projectName: SUMO a stability genomu
Investor: Czech Science Foundation
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