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

J 2013

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

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

Základní údaje

Originální název

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

Autoři

Vydání

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

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 8.808

Kód RIV

RIV/00216224:14110/13:00066405

Organizační jednotka

Lékařská fakulta

DOI

https://doi.org/10.1093/nar/gkt236

UT WoS

000319806600024

Klíčová slova anglicky

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

Štítky

podil

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 28. 4. 2014 17:40, Ing. Mgr. Věra Pospíšilíková

Anotace

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.

Návaznosti

GAP207/12/2323, projekt VaV

Název: Endonuleazová a translokázová aktivita v restričních-modifikáčních komplexéch typu I

Investor: Grantová agentura ČR, Endonuleázová a translokázová aktivita v restrikčních-modifikačních komplexech typu I

GA13-26629S, projekt VaV

Název: SUMO a stability genomu

Investor: Grantová agentura ČR, SUMO a stability genomu

Citovat

VIGAŠOVÁ, Dana; Prabha SARANGI; Peter KOLESÁR; Danusa VLASAKOVA; Zuzana SLEZÁKOVÁ; Veronika ALTMANNOVÁ; Fedor NIKULENKOV; Dorothea ANRATHER; Rainer GITH; Xiaolan ZHAO; Miroslav CHOVANEC a Lumír KREJČÍ. Lif1 SUMOylation and its role in non-homologous end-joining. Nucleic Acids Research. Oxford: Oxford Press, 2013, roč. 41, č. 10, s. 5341-5353. ISSN 0305-1048. Dostupné z: https://doi.org/10.1093/nar/gkt236.

@article{1124588,
   author = {Vigašová, Dana and Sarangi, Prabha and Kolesár, Peter and Vlasakova, Danusa and Slezáková, Zuzana and Altmannová, Veronika and Nikulenkov, Fedor and Anrather, Dorothea and Gith, Rainer and Zhao, Xiaolan and Chovanec, Miroslav and Krejčí, Lumír},
   article_location = {Oxford},
   article_number = {10},
   doi = {https://doi.org/10.1093/nar/gkt236},
   keywords = {DOUBLE-STRAND BREAKS; DNA-LIGASE-IV; SACCHAROMYCES-CEREVISIAE; CRYSTAL-STRUCTURE; FUNCTIONAL INTERACTION; REPAIR PATHWAY; YEAST SEPTINS/; MATING-TYPE; PROTEIN; SUMO},
   language = {eng},
   issn = {0305-1048},
   journal = {Nucleic Acids Research},
   title = {Lif1 SUMOylation and its role in non-homologous end-joining},
   url = {http://nar.oxfordjournals.org/content/41/10/5341.long},
   volume = {41},
   year = {2013}
}

TY  - JOUR
ID  - 1124588
AU  - Vigašová, Dana - Sarangi, Prabha - Kolesár, Peter - Vlasakova, Danusa - Slezáková, Zuzana - Altmannová, Veronika - Nikulenkov, Fedor - Anrather, Dorothea - Gith, Rainer - Zhao, Xiaolan - Chovanec, Miroslav - Krejčí, Lumír
PY  - 2013
TI  - Lif1 SUMOylation and its role in non-homologous end-joining
JF  - Nucleic Acids Research
VL  - 41
IS  - 10
SP  - 5341-5353
EP  - 5341-5353
PB  - Oxford Press
SN  - 03051048
KW  - DOUBLE-STRAND BREAKS
KW  - DNA-LIGASE-IV
KW  - SACCHAROMYCES-CEREVISIAE
KW  - CRYSTAL-STRUCTURE
KW  - FUNCTIONAL INTERACTION
KW  - REPAIR PATHWAY
KW  - YEAST SEPTINS/
KW  - MATING-TYPE
KW  - PROTEIN
KW  - SUMO
UR  - http://nar.oxfordjournals.org/content/41/10/5341.long
N2  - 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.
ER  -

VIGAŠOVÁ, Dana; Prabha SARANGI; Peter KOLESÁR; Danusa VLASAKOVA; Zuzana SLEZÁKOVÁ; Veronika ALTMANNOVÁ; Fedor NIKULENKOV; Dorothea ANRATHER; Rainer GITH; Xiaolan ZHAO; Miroslav CHOVANEC a Lumír KREJČÍ. Lif1 SUMOylation and its role in non-homologous end-joining. \textit{Nucleic Acids Research}. Oxford: Oxford Press, 2013, roč.~41, č.~10, s.~5341-5353. ISSN~0305-1048. Dostupné z: https://doi.org/10.1093/nar/gkt236.

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