2015
Sumoylation Influences DNA Break Repair Partly by Increasing the Solubility of a Conserved End Resection Protein
SARANGI, Prabha, Roland STEINACHER, Veronika ALTMANNOVÁ, Qiong FU, Tanya T. PAULL et. al.Základní údaje
Originální název
Sumoylation Influences DNA Break Repair Partly by Increasing the Solubility of a Conserved End Resection Protein
Autoři
SARANGI, Prabha (840 Spojené státy), Roland STEINACHER (826 Velká Británie a Severní Irsko), Veronika ALTMANNOVÁ (203 Česká republika, domácí), Qiong FU (840 Spojené státy), Tanya T. PAULL (840 Spojené státy), Lumír KREJČÍ (203 Česká republika, garant, domácí), Matthew WHITBY (826 Velká Británie a Severní Irsko) a Xiaolan ZHAO (840 Spojené státy)
Vydání
PLoS Genetics, San Francisco, California, United States, Public Library Science, 2015, 1553-7390
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
Genetika a molekulární biologie
Stát vydavatele
Spojené státy
Utajení
není předmětem státního či obchodního tajemství
Impakt faktor
Impact factor: 7.528 v roce 2014
Kód RIV
RIV/00216224:14110/15:00080646
Organizační jednotka
Lékařská fakulta
UT WoS
000349314600020
EID Scopus
2-s2.0-84924402458
Klíčová slova anglicky
Sumoylation; DNA Break Repair; Conserved End Resection Protein
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 9. 7. 2015 10:46, Ing. Mgr. Věra Pospíšilíková
Anotace
V originále
Protein modifications regulate both DNA repair levels and pathway choice. How each modification achieves regulatory effects and how different modifications collaborate with each other are important questions to be answered. Here, we show that sumoylation regulates double-strand break repair partly by modifying the end resection factor Sae2. This modification is conserved from yeast to humans, and is induced by DNA damage. We mapped the sumoylation site of Sae2 to a single lysine in its self-association domain. Abolishing Sae2 sumoylation by mutating this lysine to arginine impaired Sae2 function in the processing and repair of multiple types of DNA breaks. We found that Sae2 sumoylation occurs independently of its phosphorylation, and the two modifications act in synergy to increase soluble forms of Sae2. We also provide evidence that sumoylation of the Sae2-binding nuclease, the Mre11-Rad50-Xrs2 complex, further increases end resection. These findings reveal a novel role for sumoylation in DNA repair by regulating the solubility of an end resection factor. They also show that collaboration between different modifications and among multiple substrates leads to a stronger biological effect.
Návaznosti
EE2.3.30.0009, projekt VaV |
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GAP207/12/2323, projekt VaV |
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GA13-26629S, projekt VaV |
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