Show simple item record

Files in this item

Thumbnail

Item metadata

dc.contributor.authorSeeler, Jacob-S
dc.contributor.authorMarchio, Agnes
dc.contributor.authorLosson, Regine
dc.contributor.authorDesterro, Joana M P
dc.contributor.authorHay, Ronald Thomas
dc.contributor.authorChambon, Pierre
dc.contributor.authorDejean, Anne
dc.date.accessioned2014-07-04T11:31:02Z
dc.date.available2014-07-04T11:31:02Z
dc.date.issued2001-05
dc.identifier.citationSeeler , J-S , Marchio , A , Losson , R , Desterro , J M P , Hay , R T , Chambon , P & Dejean , A 2001 , ' Common properties of the nuclear body protein SP100 and the TIF1alpha chromatin factor: the role of SUMO modification ' , Molecular and Cellular Biology , vol. 21 , no. 10 , pp. 3314-3324 . https://doi.org/10.1128/MCB.21.10.3314-3324.2001en
dc.identifier.issn0270-7306
dc.identifier.otherPURE: 155579
dc.identifier.otherPURE UUID: 4afd88a9-24ee-43aa-a186-1dc7a0d654b1
dc.identifier.otherWOS: 000168306700004
dc.identifier.otherScopus: 0035028618
dc.identifier.urihttp://hdl.handle.net/10023/4944
dc.descriptionThis work was supported by grants from the European Community, the Association for International Cancer Research, and the Association pour la Recherche sur le Cancer.en
dc.description.abstractThe SP100 protein, together with PML, represents a major constituent of the PML-SP100 nuclear bodies (NBs). The function of these ubiquitous subnuclear structures, whose integrity is compromised in pathological situations such as acute promyelocytic leukemia (APL) or DNA virus infection, remains poorly understood. There is little evidence for the occurrence of actual physiological processes within NBs. The two NE proteins PML and SP100 are covalently modified by the ubiquitin-related SUMO-1 modifier, and recent work indicates that this modification is critical for the regulation of NE dynamics. In exploring the functional relationships between NBs and chromatin, we have shown previously that SP100 interacts with members of the HP1 family of nonhistone chromosomal proteins and that a variant SP100 cDNA encodes a high-mobility group (HMG1/2) protein. Here we report the isolation of a further cDNA, encoding the SP100C protein, that contains the PHD-bromodomain motif characteristic of chromatin proteins. We further show that TIF1 alpha, a chromatin-associated factor with homology to both PML and SP100C, is also modified by SUMO-1. Finally, in vitro experiments indicate that SUMO modification of SP100 enhances the stability of SP100-HP1 complexes. Taken together, our results suggest an association of SP100 and its variants with the chromatin compartment and, further, indicate that SUMO modification may play a regulatory role in the functional interplay between the nuclear bodies and chromatin.
dc.format.extent11
dc.language.isoeng
dc.relation.ispartofMolecular and Cellular Biologyen
dc.rightsCopyright © 2001, American Society for Microbiology. All Rights Reserved. Open Access article available from PMC.en
dc.subjectAcute promyelocytic leukemiaen
dc.subjectPrimary biliary-cirrhosisen
dc.subjectZinc-finger proteinsen
dc.subjectPml-rar-alphaen
dc.subjectCovalent modificationen
dc.subjectTranscriptional coactivatoren
dc.subjectRepressor domainen
dc.subjectBinding-proteinen
dc.subjectPore complexen
dc.subjectHP1 proteinsen
dc.subjectQR Microbiologyen
dc.subject.lccQRen
dc.titleCommon properties of the nuclear body protein SP100 and the TIF1alpha chromatin factor: the role of SUMO modificationen
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews.School of Biologyen
dc.identifier.doihttps://doi.org/10.1128/MCB.21.10.3314-3324.2001
dc.description.statusPeer revieweden
dc.identifier.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC100253/en


This item appears in the following Collection(s)

Show simple item record