A Lorenz

A Ray Chaudhuri

Alexander Lorenz

B Pfander

B Xhemalce

CL Doe

Claire Bryer

CP Lin

D Branzei

E Papouli

EA Andrews

F Golebiowski

F Osman

F Wei

Fekret Osman

FZ Watts

G Gill

G Rosas-Acosta

H Sun

HD Ulrich

J Bähler

J Heideker

J Prudden

JJ Champoux

JR Mullen

JS Ahn

K Horie

K Mizuno

K Uzunova

L Roseaulin

M Berti

M Kai

M Regairaz

Matthew C. Whitby

MC Geoffroy

MH Tatham

Michael Lichten

P Burkovics

P D'Arpa

Q Cai

R Steinacher

RC Burgess

Roland Steinacher

S Bergink

S Codlin

S Jentsch

S Lambert

S Moreno

S Squires

SD Desai

SP Jackson

T Hunter

T Ii

T Inagawa

T Schleker

TK Li

U Hardeland

VG Panse

W Sun

XL Chen

Y Galanty

Y Mao

Y Matsuo

Y Xie

PLoS ONE

English

PubMed

The SUMO-dependent ubiquitin ligase Slx8 plays key roles in promoting genome stability, including the processing of trapped Topoisomerase I (Top1) cleavage complexes and removal of toxic SUMO conjugates. We show that it is the latter function that constitutes Slx8’s primary role in fission yeast. The SUMO conjugates in question are formed by the SUMO ligase Pli1, which is necessary for limiting spontaneous homologous recombination when Top1 is present. Surprisingly there is no requirement for Pli1 to limit recombination in the vicinity of a replication fork blocked at the programmed barrier RTS1. Notably, once committed to Pli1-mediated SUMOylation Slx8 becomes essential for genotoxin resistance, limiting both spontaneous and RTS1 induced recombination, and promoting normal chromosome segregation. We show that Slx8 removes Pli1-dependent Top1-SUMO conjugates and in doing so helps to constrain recombination at RTS1. Overall our data highlight how SUMOylation and SUMO-dependent ubiquitylation by the Pli1-Slx8 axis contribute in different ways to maintain genome stability

Er Lorenz

CiteSeerX

Slx8 Removes Pli1-Dependent Protein-SUMO Conjugates Including SUMOylated Topoisomerase I to Promote Genome Stability

The SUMO-dependent ubiquitin ligase Slx8 plays key roles in promoting genome stability, including the processing of trapped Topoisomerase I (Top1) cleavage complexes and removal of toxic SUMO conjugates. We show that it is the latter function that constitutes Slx8's primary role in fission yeast. The SUMO conjugates in question are formed by the SUMO ligase Pli1, which is necessary for limiting spontaneous homologous recombination when Top1 is present. Surprisingly there is no requirement for Pli1 to limit recombination in the vicinity of a replication fork blocked at the programmed barrier RTS1. Notably, once committed to Pli1-mediated SUMOylation Slx8 becomes essential for genotoxin resistance, limiting both spontaneous and RTS1 induced recombination, and promoting normal chromosome segregation. We show that Slx8 removes Pli1-dependent Top1-SUMO conjugates and in doing so helps to constrain recombination at RTS1. Overall our data highlight how SUMOylation and SUMO-dependent ubiquitylation by the Pli1-Slx8 axis contribute in different ways to maintain genome stability

Matthew C Whitby

Directory of Open Access Journals

Slx8 removes Pli1-dependent protein-SUMO conjugates including SUMOylated topoisomerase I to promote genome stability.

Steinacher, Roland

Osman, Fekret

Lorenz, Alexander

Bryer, Claire

Whitby, Matthew C

The Open University

Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover.

Posttranslational modifications of repair factors and histones in the cellular response to stalled replication forks.

Regulation of DNA damage responses by ubiquitin and SUMO.

Regulatory Functions of Ubiquitin and

Role of SUMO in the dynamics of telomere maintenance in fission yeast.

Scha ¨r P

Scho ¨ler HR,

SUMO and ubiquitin in the nucleus: different functions, similar mechanisms?

SUMO keeps a check on recombination during DNA replication.

The role of Schizosaccharomyces pombe SUMO ligases in genome stability.

Ubiquitin/SUMO modification regulates VHL protein stability and nucleocytoplasmic localization.

Slx8 removes Pli1-dependent protein-SUMO conjugates including SUMOylated Topoisomerase I to promote genome stability

<div><p>The SUMO-dependent ubiquitin ligase Slx8 plays key roles in promoting genome stability, including the processing of trapped Topoisomerase I (Top1) cleavage complexes and removal of toxic SUMO conjugates. We show that it is the latter function that constitutes Slx8's primary role in fission yeast. The SUMO conjugates in question are formed by the SUMO ligase Pli1, which is necessary for limiting spontaneous homologous recombination when Top1 is present. Surprisingly there is no requirement for Pli1 to limit recombination in the vicinity of a replication fork blocked at the programmed barrier <i>RTS1</i>. Notably, once committed to Pli1-mediated SUMOylation Slx8 becomes essential for genotoxin resistance, limiting both spontaneous and <i>RTS1</i> induced recombination, and promoting normal chromosome segregation. We show that Slx8 removes Pli1-dependent Top1-SUMO conjugates and in doing so helps to constrain recombination at <i>RTS1</i>. Overall our data highlight how SUMOylation and SUMO-dependent ubiquitylation by the Pli1-Slx8 axis contribute in different ways to maintain genome stability.</p></div

Slx8 removes Pli1-dependent protein-SUMO conjugates including SUMOylated Topoisomerase I to promote genome stability

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