J 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

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
Name: Zaměstnáním čerstvých absolventů doktorského studia k vědecké excelenci
GAP207/12/2323, research and development project
Name: Endonuleazová a translokázová aktivita v restričních-modifikáčních komplexéch typu I
Investor: Czech Science Foundation
GA13-26629S, research and development project
Name: SUMO a stability genomu
Investor: Czech Science Foundation