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Article: SUMO chain formation is required for response to replication arrest in S. pombe

TitleSUMO chain formation is required for response to replication arrest in S. pombe
Authors
Issue Date2009
PublisherPublic Library of Science. The Journal's web site is located at http://www.plosone.org/home.action
Citation
P L o S One, 2009, v. 4 n. 8, p. e6750 How to Cite?
AbstractSUMO is a ubiquitin-like protein that is post-translationally attached to one or more lysine residues on target proteins. Despite having only 18% sequence identity with ubiquitin, SUMO contains the conserved betabetaalphabetabetaalphabeta fold present in ubiquitin. However, SUMO differs from ubiquitin in having an extended N-terminus. In S. pombe the N-terminus of SUMO/Pmt3 is significantly longer than those of SUMO in S. cerevisiae, human and Drosophila. Here we investigate the role of this N-terminal region. We have used two dimensional gel electrophoresis to demonstrate that S. pombe SUMO/Pmt3 is phosphorylated, and that this occurs on serine residues at the extreme N-terminus of the protein. Mutation of these residues (in pmt3-1) results in a dramatic reduction in both the levels of high Mr SUMO-containing species and of total SUMO/Pmt3, indicating that phosphorylation of SUMO/Pmt3 is required for its stability. Despite the significant reduction in high Mr SUMO-containing species, pmt3-1 cells do not display an aberrant cell morphology or sensitivity to genotoxins or stress. Additionally, we demonstrate that two lysine residues in the N-terminus of S. pombe SUMO/Pmt3 (K14 and K30) can act as acceptor sites for SUMO chain formation in vitro. Inability to form SUMO chains results in aberrant cell and nuclear morphologies, including stretched and fragmented chromatin. SUMO chain mutants are sensitive to the DNA synthesis inhibitor, hydroxyurea (HU), but not to other genotoxins, such as UV, MMS or CPT. This implies a role for SUMO chains in the response to replication arrest in S. pombe.
Persistent Identifierhttp://hdl.handle.net/10722/132165
ISSN
2015 Impact Factor: 3.057
2015 SCImago Journal Rankings: 1.395
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorSkilton, A-
dc.contributor.authorHo, JCY-
dc.contributor.authorMercer, B-
dc.contributor.authorOutwin, E-
dc.contributor.authorWatts, FZ-
dc.date.accessioned2011-03-18T06:41:35Z-
dc.date.available2011-03-18T06:41:35Z-
dc.date.issued2009-
dc.identifier.citationP L o S One, 2009, v. 4 n. 8, p. e6750-
dc.identifier.issn1932-6203-
dc.identifier.urihttp://hdl.handle.net/10722/132165-
dc.description.abstractSUMO is a ubiquitin-like protein that is post-translationally attached to one or more lysine residues on target proteins. Despite having only 18% sequence identity with ubiquitin, SUMO contains the conserved betabetaalphabetabetaalphabeta fold present in ubiquitin. However, SUMO differs from ubiquitin in having an extended N-terminus. In S. pombe the N-terminus of SUMO/Pmt3 is significantly longer than those of SUMO in S. cerevisiae, human and Drosophila. Here we investigate the role of this N-terminal region. We have used two dimensional gel electrophoresis to demonstrate that S. pombe SUMO/Pmt3 is phosphorylated, and that this occurs on serine residues at the extreme N-terminus of the protein. Mutation of these residues (in pmt3-1) results in a dramatic reduction in both the levels of high Mr SUMO-containing species and of total SUMO/Pmt3, indicating that phosphorylation of SUMO/Pmt3 is required for its stability. Despite the significant reduction in high Mr SUMO-containing species, pmt3-1 cells do not display an aberrant cell morphology or sensitivity to genotoxins or stress. Additionally, we demonstrate that two lysine residues in the N-terminus of S. pombe SUMO/Pmt3 (K14 and K30) can act as acceptor sites for SUMO chain formation in vitro. Inability to form SUMO chains results in aberrant cell and nuclear morphologies, including stretched and fragmented chromatin. SUMO chain mutants are sensitive to the DNA synthesis inhibitor, hydroxyurea (HU), but not to other genotoxins, such as UV, MMS or CPT. This implies a role for SUMO chains in the response to replication arrest in S. pombe.-
dc.languageeng-
dc.publisherPublic Library of Science. The Journal's web site is located at http://www.plosone.org/home.action-
dc.relation.ispartofP L o S One-
dc.subject.meshDNA Damage-
dc.subject.meshElectrophoresis, Gel, Two-Dimensional-
dc.subject.meshHydroxyurea - pharmacology-
dc.subject.meshSchizosaccharomyces - cytology - drug effects-
dc.subject.meshSmall Ubiquitin-Related Modifier Proteins - chemistry - physiology-
dc.titleSUMO chain formation is required for response to replication arrest in S. pombeen_US
dc.typeArticleen_US
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1932-6203&volume=4&issue=8&spage=e6750&epage=&date=2009&atitle=SUMO+chain+formation+is+required+for+response+to+replication+arrest+in+S.+pombe-
dc.identifier.emailHo, JCY: jennyho@hku.hk-
dc.identifier.emailWatts, FZ: f.z.watts@sussex.ac.uk-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1371/journal.pone.0006750-
dc.identifier.pmid19707600-
dc.identifier.pmcidPMC2727700-
dc.identifier.scopuseid_2-s2.0-69849114721-
dc.identifier.hkuros174099-
dc.identifier.volume4-
dc.identifier.issue8-
dc.identifier.spagee6750-
dc.identifier.isiWOS:000269278400015-

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