Detailed Information on Publication Record
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.Basic information
Original name
Sumoylation Influences DNA Break Repair Partly by Increasing the Solubility of a Conserved End Resection Protein
Authors
SARANGI, Prabha (840 United States of America), Roland STEINACHER (826 United Kingdom of Great Britain and Northern Ireland), Veronika ALTMANNOVÁ (203 Czech Republic, belonging to the institution), Qiong FU (840 United States of America), Tanya T. PAULL (840 United States of America), Lumír KREJČÍ (203 Czech Republic, guarantor, belonging to the institution), Matthew WHITBY (826 United Kingdom of Great Britain and Northern Ireland) and Xiaolan ZHAO (840 United States of America)
Edition
PLoS Genetics, San Francisco, California, United States, Public Library Science, 2015, 1553-7390
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
Genetics and molecular biology
Country of publisher
United States of America
Confidentiality degree
není předmětem státního či obchodního tajemství
Impact factor
Impact factor: 7.528 in 2014
RIV identification code
RIV/00216224:14110/15:00080646
Organization unit
Faculty of Medicine
UT WoS
000349314600020
Keywords in English
Sumoylation; DNA Break Repair; Conserved End Resection Protein
Tags
International impact, Reviewed
Změněno: 9/7/2015 10:46, Ing. Mgr. Věra Pospíšilíková
Abstract
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.
Links
EE2.3.30.0009, research and development project |
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GAP207/12/2323, research and development project |
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GA13-26629S, research and development project |
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