PXD011953 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Stn1 S74 phosphorylation - Telomeres, the protective ends of eukaryotic chromosomes, are replicated through concerted actions by conventional DNA polymerases and telomerase, though the regulation of this process is not fully understood |
Description | Publication abstract: Telomeres, the protective ends of eukaryotic chromosomes, are replicated through concerted actions by conventional DNA polymerases and telomerase, though the regulation of this process is not fully understood. Telomere replication requires (C)-Stn1-Ten1, a telomere ssDNA-binding complex that is homologous to RPA. Here, we show that the evolutionarily conserved phosphatase Ssu72 is responsible for terminating the cycle of telomere replication in fission yeast. Ssu72 controls the recruitment of Stn1 to telomeres by regulating Stn1 phosphorylation at S74, a residue that lies within the conserved OB fold domain. Consequently, ssu72Δ mutants are defective in telomere replication and exhibit long 3′ overhangs, which are indicative of defective lagging strand DNA synthesis. We also show that hSSU72 regulates telomerase activation in human cells by controlling the recruitment of hSTN1 to telomeres. Thus, in this study, we demonstrate a previously unknown yet conserved role for the phosphatase SSU72, whereby this enzyme controls telomere homeostasis by activating lagging strand DNA synthesis, thus terminating the cycle of telomere replication. Summary of MS experiment: Stn1 protein was tagged in the C-terminus with 13-myc tag and purified by immunoprecipitation. The purified extracts were separated by SDS-PAGE and proteins between 63 and 75 kDa were excised and in-gel digested. Tryptic peptides were analyzed by LC-MS/MS using an AB Sciex TripleTOF 6600 mass spectrometer upon separation by nanoLC-MS using an Ekspert 425 nanoLC with cHiPLC. Stn1 protein was identified with 48% of coverage and Serine-74 was found to be phosphorylated. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_04:51:08.923.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Inês M. Luís |
SpeciesList | scientific name: Schizosaccharomyces pombe 927; NCBI TaxID: 1264690; |
ModificationList | S-carboxamidoethyl-L-cysteine; phosphorylated residue |
Instrument | TripleTOF 6600 |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2018-12-06 01:53:14 | ID requested | |
1 | 2019-02-19 09:05:43 | announced | |
2 | 2020-03-12 03:46:34 | announced | 2020-03-12: Updated project metadata. |
⏵ 3 | 2024-10-22 04:51:09 | announced | 2024-10-22: Updated project metadata. |
Publication List
Dataset with its publication pending |
Keyword List
curator keyword: Biological |
submitter keyword: Schizosaccharomyces pombe,Fission yeast, Telomere replication |
Contact List
Isabel A. Abreu |
contact affiliation | ITQB NOVA, Oeiras, Portugal |
contact email | abreu@itqb.unl.pt |
lab head | |
Inês M. Luís |
contact affiliation | ITQB NOVA |
contact email | imluis@itqb.unl.pt |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
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- PRIDE
- PXD011953
- Label: PRIDE project
- Name: Stn1 S74 phosphorylation - Telomeres, the protective ends of eukaryotic chromosomes, are replicated through concerted actions by conventional DNA polymerases and telomerase, though the regulation of this process is not fully understood