Dataset Information

SUMOylation regulates Lem2 function in centromere clustering and silencing.

ABSTRACT: Regulation by the small modifier SUMO is heavily dependent on spatial control of enzymes that mediate the attachment and removal of SUMO on substrate proteins. Here we show that in fission yeast, delocalisation of the SUMO protease Ulp1 from the nuclear envelope results in centromeric defects that can be attributed to hyper-SUMOylation at the nuclear periphery. Unexpectedly, we find that while this localised hyper-SUMOylation impairs centromeric silencing, it can also enhance centromere clustering. Moreover, both effects are at least partially dependent on SUMOylation of the inner nuclear membrane protein Lem2. Lem2 has previously been implicated in diverse biological processes, including the promotion of both centromere clustering and silencing, but how these distinct activities are coordinated was unclear; our observations suggest a model whereby SUMOylation may serve as a regulatory switch, modulating Lem2 interactions with competing partner proteins to balance its roles in alternative pathways. Our findings also reveal a previously unappreciated role for SUMOylation in promoting centromere clustering.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Schizosaccharomyces Pombe 927

TISSUE(S): Cell Culture

SUBMITTER: Joanna Strachan

LAB HEAD: Elizabeth Bayne

PROVIDER: PXD046003 | Pride | 2023-11-20

REPOSITORIES: Pride

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			Action	DRS
	Strachan_Etal_2023_WT_Group6_F1_F8.7z	Other
	Strachan_etal_2023_WT_Group1_B1.raw	Raw
	Strachan_etal_2023_WT_Group1_B1_B8.7z	Other
	Strachan_etal_2023_WT_Group1_B2.raw	Raw
	Strachan_etal_2023_WT_Group1_B3.raw	Raw

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SUMOylation regulates Lem2 function in centromere clustering and silencing.

Strachan Joanna J Leidecker Orsolya O Spanos Christos C Le Coz Clementine C Chapman Elliott E Arsenijevic Ana A Zhang Haidao H Zhao Ning N Spoel Steven H SH Bayne Elizabeth H EH

Journal of cell science 20231201 23

Regulation by the small modifier SUMO is heavily dependent on spatial control of enzymes that mediate the attachment and removal of SUMO on substrate proteins. Here, we show that in the fission yeast Schizosaccharomyces pombe, delocalisation of the SUMO protease Ulp1 from the nuclear envelope results in centromeric defects that can be attributed to hyper-SUMOylation at the nuclear periphery. Unexpectedly, we find that although this localised hyper-SUMOylation impairs centromeric silencing, it ca ...[more]

PMID: 37970674

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Project description:Genotoxic agents can cause replication fork stalling in dividing cells due to DNA lesions, eventually leading to replication fork collapse when the damage is not repaired. Small Ubiquitin-like Modifiers (SUMOs) are known to counteract replication stress, nevertheless, only a small number of relevant SUMO target proteins are known. To address this, we have purified and identified SUMO-2 target proteins regulated by replication stress in human cells. The developed methodology enabled single step purification of His10-SUMO-2 conjugates under denaturing conditions with high yield and high purity. The methodology is generic and is widely applicable in the ubiquitin field. Following statistical analysis on five biological replicates, a total of 566 SUMO-2 targets were identified. After 2 hours of Hydroxyurea treatment, 10 proteins were up-regulated for SUMOylation and 2 proteins were down-regulated for SUMOylation, whereas after 24 hours, 35 proteins were up-regulated for SUMOylation and 13 proteins were down-regulated for SUMOylation. A site-specific approach was used to map over 1,000 SUMO-2 acceptor lysines in target proteins. A large subset of these identified proteins function in one network that consists of interacting replication factors, transcriptional regulators, DNA damage response factors including MDC1, ATR-interacting protein ATRIP, the Bloom syndrome protein and the BLM-binding partner RMI1, the crossover junction endonuclease EME1, BRCA1 and CHAF1A. Furthermore, centromeric proteins and signal transducers were dynamically regulated by SUMOylation upon replication stress. Our results uncover a comprehensive network of SUMO target proteins dealing with replication damage and provide a framework for detailed understanding of the role of SUMOylation to counteract replication stress. Ultimately, our study reveals how a post-translational modification is able to orchestrate a large variety of different proteins to integrate different nuclear processes with the aim of dealing with the induced DNA damage

Dataset Information

SUMOylation regulates Lem2 function in centromere clustering and silencing.

Dataset's files

Publications

SUMOylation regulates Lem2 function in centromere clustering and silencing.

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