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The fission yeast Stn1-Ten1 complex limits telomerase activity via its SUMO-interacting motif and promotes telomeres replication

2018-05-16Journal article Restricted access
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dc.contributor.authorMatmati, Samah
dc.contributor.authorVaurs, Mélina
dc.contributor.authorEscandell, José M
dc.contributor.authorMaestroni, Laetitia
dc.contributor.authorNakamura, Toru M
dc.contributor.authorFerreira, Miguel G
dc.contributor.authorGéli, Vincent
dc.contributor.authorCoulon, Stéphane
dc.date.accessioned2018-05-21T11:17:45Z
dc.date.available2018-05-21T11:17:45Z
dc.date.issued2018-05-16
dc.descriptionThis deposit is composed by a publication in which the IGC's authors have had the role of collaboration (it's a collaboration publication). This type of deposit in ARCA is in restrictedAccess (it can't be in open access to the public), and can only be accessed by two ways: either by requesting a legal copy from the author (the email contact present in this deposit) or by visiting the following link: http://advances.sciencemag.org/content/4/5/eaar2740.fullpt_PT
dc.description.abstractMammalian CST (CTC1-STN1-TEN1) complex fulfills numerous functions including rescue of the stalled replication forks and termination of telomerase action. In fission yeast lacking the CTC1 ortholog, the Stn1-Ten1 complex restricts telomerase action via its sumoylation-mediated interaction with Tpz1TPP1. We identify a small ubiquitin-like modifier (SUMO)-interacting motif (SIM) in the carboxyl-terminal part of Stn1 and show that this domain is crucial for SUMO and Tpz1-SUMO interactions. Point mutations in the SIM (Stn1-226) lead to telomere elongation, impair Stn1-Ten1 recruitment to telomeres, and enhance telomerase binding, revealing that Stn1 SIM domain contributes to the inhibition of telomerase activity at chromosome ends. Our results suggest that Stn1-Ten1 promotes DNA synthesis at telomeres to limit single-strand DNA accumulation. We further demonstrate that Stn1 functions in the replication of telomeric and subtelomeric regions in a Taz1-independent manner. Genetic analysis reveals that misregulation of origin firing and/or telomerase inhibition circumvents the replication defects of the stn1-226 mutant. Together, our results show that the Stn1-Ten1 complex has a dual function at telomeres by limiting telomerase action and promoting chromosome end replication.pt_PT
dc.description.sponsorshipThe VG laboratory is supported by the Ligue Nationale Contre le Cancer (LNCC) (Equipe Labéllisée) and by the Agence Nationale de la Recherche (ANR-Blanc Quiescence DNA SVSE8). S.C. is supported by Projet Fondation ARC. S.M. is supported by the LNCC and L.M. is supported by the ANR-Blanc Quiescence DNA SVSE8. T.M.N. is supported by the NIH grant no. R01GM078253. M.G.F and J.M.E are supported by Portuguese Fundação para a Ciência e a Tecnologia grant PTDC/BEX-BCM/5179/14.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationS. Matmati, M. Vaurs, J. M. Escandell, L. Maestroni, T. M. Nakamura, M. G. Ferreira, V. Géli, S. Coulon, The fission yeast Stn1-Ten1 complex limits telomerase activity via its SUMOinteracting motif and promotes telomeres replication. Sci. Adv. 4, eaar2740 (2018).pt_PT
dc.identifier.doi10.1126/sciadv.aar2740pt_PT
dc.identifier.urihttp://hdl.handle.net/10400.7/878
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherAmerican Association for the Advancement of Sciencept_PT
dc.relationR01GM078253pt_PT
dc.relationPTDC/BEX-BCM/5179/14pt_PT
dc.relation.publisherversionhttp://advances.sciencemag.org/content/4/5/eaar2740pt_PT
dc.rights.urihttp://creativecommons.org/licenses/by-nc/4.0/pt_PT
dc.subjectCST Complexpt_PT
dc.subjecttelomerasept_PT
dc.subjectSUMO-interactingpt_PT
dc.subjectStn1-Ten1 complexpt_PT
dc.subjectchromosomept_PT
dc.subjectreplicationpt_PT
dc.subjectDNA replicationpt_PT
dc.subjectTaz1pt_PT
dc.subjectStn1 proteinpt_PT
dc.subjectfission yeastpt_PT
dc.titleThe fission yeast Stn1-Ten1 complex limits telomerase activity via its SUMO-interacting motif and promotes telomeres replicationpt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage14pt_PT
oaire.citation.issue5pt_PT
oaire.citation.startPage1pt_PT
oaire.citation.titleScience Advancespt_PT
oaire.citation.volume4pt_PT
rcaap.rightsrestrictedAccesspt_PT
rcaap.typearticlept_PT

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