Nuclear distribution of prothymosin alpha and parathymosin: evidence that prothymosin alpha is associated with RNA synthesis processing and parathymosin with early DNA replication

dc.contributor.authorVareli, K.en
dc.contributor.authorFrangou-Lazaridis, M.en
dc.contributor.authorvan der Kraan, I.en
dc.contributor.authorTsolas, O.en
dc.contributor.authorvan Driel, R.en
dc.date.accessioned2015-11-24T19:01:24Z
dc.date.available2015-11-24T19:01:24Z
dc.identifier.issn0014-4827-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/19686
dc.rightsDefault Licence-
dc.subjectCell Nucleus/genetics/*metabolismen
dc.subject*DNA Replicationen
dc.subjectHumansen
dc.subjectProtein Precursors/*metabolismen
dc.subjectRNA/*biosynthesisen
dc.subjectThymosin/*analogs & derivatives/metabolismen
dc.subjectTumor Cells, Cultureden
dc.titleNuclear distribution of prothymosin alpha and parathymosin: evidence that prothymosin alpha is associated with RNA synthesis processing and parathymosin with early DNA replicationen
heal.abstractProthymosin alpha and parathymosin are two ubiquitous small acidic nuclear proteins that are thought to be involved in cell cycle progression, proliferation, and cell differentiation. In an effort to investigate the molecular function of the two proteins, we studied their spatial distribution by indirect immunofluorescence labeling and confocal scanning laser microscopy in relation to nuclear components involved in transcription, translation, and splicing. Results indicate that both proteins exhibit a punctuated nuclear distribution and are excluded by nucleoli. The distribution of prothymosin alpha in the nucleus is related to that of transcription sites, whereas the distribution of parathymosin correlates with early replication sites. This implies that prothymosin alpha and parathymosin are involved in transcription and replication, respectively. In addition to the punctate distribution, prothymosin alpha also is found concentrated in 1-6 nuclear domains per cell. These domains are found in more than 80% of randomly growing T24 human bladder carcinoma cells. They have a diameter of 0.2-2.5 microm, their size being inversely related to the number of domains per cell. The domains disappear during mitosis and the protein is excluded from the metaphase chromosomes. Double-labeling experiments associate these prothymosin alpha domains with PML and CstF64 containing nuclear bodies, but not with hnRNP-I containing domains or coiled bodies.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.primary10.1006/excr.2000.4857-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/10854063-
heal.identifier.secondaryhttp://ac.els-cdn.com/S0014482700948572/1-s2.0-S0014482700948572-main.pdf?_tid=d4d128a73e79e04f1653e861a93c929a&acdnat=1337849249_002561cc2950928acaeb56648779dc1c-
heal.journalNameExp Cell Resen
heal.journalTypepeer-reviewed-
heal.languageen-
heal.publicationDate2000-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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