Näytä suppeat kuvailutiedot

dc.contributor.authorViiri, Keijo
dc.contributor.authorKorkeamäki, Hanna
dc.contributor.authorKukkonen, Mari
dc.contributor.authorNieminen, Laura
dc.contributor.authorLindfors, Katri
dc.contributor.authorPeterson, Pert
dc.contributor.authorMäki, Markku
dc.contributor.authorKainulainen, Heikki
dc.contributor.authorLohi, Olli
dc.date.accessioned2022-08-25T06:09:43Z
dc.date.available2022-08-25T06:09:43Z
dc.date.issued2006
dc.identifier.citationViiri, K., Korkeamäki, H., Kukkonen, M., Nieminen, L., Lindfors, K., Peterson, P., Mäki, M., Kainulainen, H., & Lohi, O. (2006). SAP30L interacts with members of the Sin3A corepressor complex and targets Sin3A to the nucleolus. <i>Nucleic Acids Research</i>, <i>34</i>(11), 3288-3298. <a href="https://doi.org/10.1093/nar/gkl401" target="_blank">https://doi.org/10.1093/nar/gkl401</a>
dc.identifier.otherCONVID_16174979
dc.identifier.otherTUTKAID_21326
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/82811
dc.description.abstractHistone acetylation plays a key role in the regulation of gene expression. The chromatin structure and accessibility of genes to transcription factors is regulated by enzymes that acetylate and deacetylate histones. The Sin3A corepressor complex recruits histone deacetylases and in many cases represses transcription. Here, we report that SAP30L, a close homolog of Sin3-associated protein 30 (SAP30), interacts with several components of the Sin3A corepressor complex. We show that it binds to the PAH3/HID (Paired Amphipathic Helix 3/Histone deacetylase Interacting Domain) region of mouse Sin3A with residues 120–140 in the C-terminal part of the protein. We provide evidence that SAP30L induces transcriptional repression, possibly via recruitment of Sin3A and histone deacetylases. Finally, we characterize a functional nucleolar localization signal in SAP30L and show that SAP30L and SAP30 are able to target Sin3A to the nucleolus.en
dc.format.mimetypeapplication/pdf
dc.language.isoeng
dc.publisherOxford University Press
dc.relation.ispartofseriesNucleic Acids Research
dc.rightsCC BY-NC 2.0 UK
dc.subject.otherhistonideasetylaatio
dc.subject.othertumajyvänen
dc.subject.otherSin-assosioituvat proteiinit
dc.subject.otherHistone deacetylation
dc.subject.othernucleolus
dc.subject.otherSin-associated proteins
dc.titleSAP30L interacts with members of the Sin3A corepressor complex and targets Sin3A to the nucleolus
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-202208254344
dc.contributor.laitosLiikuntabiologian laitosfi
dc.contributor.laitosDepartment of Biology of Physical Activityen
dc.contributor.oppiaineLiikuntafysiologiafi
dc.contributor.oppiaineExercise Physiologyen
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.type.coarhttp://purl.org/coar/resource_type/c_2df8fbb1
dc.description.reviewstatuspeerReviewed
dc.format.pagerange3288-3298
dc.relation.issn0305-1048
dc.relation.numberinseries11
dc.relation.volume34
dc.type.versionpublishedVersion
dc.rights.copyright© 2006 The Author(s).
dc.rights.accesslevelopenAccessfi
dc.subject.ysovuorovaikutus
dc.subject.ysogeenit
dc.subject.ysotranskriptio (biologia)
dc.subject.ysoproteiinit
dc.subject.ysobiokemia
dc.subject.ysoentsyymit
dc.format.contentfulltext
jyx.subject.urihttp://www.yso.fi/onto/yso/p10591
jyx.subject.urihttp://www.yso.fi/onto/yso/p147
jyx.subject.urihttp://www.yso.fi/onto/yso/p2788
jyx.subject.urihttp://www.yso.fi/onto/yso/p4332
jyx.subject.urihttp://www.yso.fi/onto/yso/p1375
jyx.subject.urihttp://www.yso.fi/onto/yso/p4769
dc.rights.urlhttps://creativecommons.org/licenses/by-nc/2.0/uk/
dc.relation.doi10.1093/nar/gkl401
jyx.fundinginformationThis work was supported by the Academy of Finland Research Council for Health (funding decision number 201361), the Foundation for Paediatric Research in Finland, the Medical Research Fund of Pirkanmaa Hospital District, Maud Kuistila Memorial Foundation, and Nona and Kullervo Väre Foundation. Funding to pay the Open Access publication charges for this article was provided by Medical Research Fund of Pirkanmaa Hospital District.
dc.type.okmA1


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