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dc.contributor.authorAlbert, Benjamin
dc.contributor.authorColleran, Christine
dc.contributor.authorLéger-Silvestre, Isabelle
dc.contributor.authorBerger, Axel B.
dc.contributor.authorDez, Christophe
dc.contributor.authorNormand, Christophe
dc.contributor.authorPerez-Fernandez, Jorge
dc.contributor.authorMcStay, Brian
dc.contributor.authorGadal, Olivier
dc.date.accessioned2018-09-20T15:59:18Z
dc.date.available2018-09-20T15:59:18Z
dc.date.issued2013-09-09
dc.identifier.citationAlbert, Benjamin; Colleran, Christine; Léger-Silvestre, Isabelle; Berger, Axel B. Dez, Christophe; Normand, Christophe; Perez-Fernandez, Jorge; McStay, Brian; Gadal, Olivier (2013). Structure-function analysis of hmo1 unveils an ancestral organization of hmg-box factors involved in ribosomal dna transcription from yeast to human. Nucleic Acids Research 41 (22), 10135-10149
dc.identifier.issn1362-4962,0305-1048
dc.identifier.urihttp://hdl.handle.net/10379/10180
dc.description.abstractRibosome biogenesis is a major metabolic effort for growing cells. In Saccharomyces cerevisiae, Hmo1, an abundant high-mobility group box protein (HMGB) binds to the coding region of the RNA polymerase I transcribed ribosomal RNAs genes and the promoters of similar to 70% of ribosomal protein genes. In this study, we have demonstrated the functional conservation of eukaryotic HMGB proteins involved in ribosomal DNA (rDNA) transcription. We have shown that when expressed in budding yeast, human UBF1 and a newly identified Sp-Hmo1 (Schizosaccharomyces pombe) localize to the nucleolus and suppress growth defect of the RNA polymerase I mutant rpa49-Delta. Owing to the multiple functions of both proteins, Hmo1 and UBF1 are not fully interchangeable. By deletion and domains swapping in Hmo1, we identified essential domains that stimulate rDNA transcription but are not fully required for stimulation of ribosomal protein genes expression. Hmo1 is organized in four functional domains: a dimerization module, a canonical HMGB motif followed by a conserved domain and a C-terminal nucleolar localization signal. We propose that Hmo1 has acquired species-specific functions and shares with UBF1 and Sp-Hmo1 an ancestral function to stimulate rDNA transcription.
dc.publisherOxford University Press (OUP)
dc.relation.ispartofNucleic Acids Research
dc.subjectrna-polymerase-i
dc.subjectupstream binding-factor
dc.subjectsaccharomyces-cerevisiae
dc.subjectfactor ubf
dc.subjectnucleolar transcription
dc.subjectfission yeast
dc.subjectgene-transcription
dc.subjectrdna transcription
dc.subjectprotein genes
dc.subjectsubunit
dc.titleStructure-function analysis of hmo1 unveils an ancestral organization of hmg-box factors involved in ribosomal dna transcription from yeast to human
dc.typeArticle
dc.identifier.doi10.1093/nar/gkt770
dc.local.publishedsourcehttp://doi.org/10.1093/nar/gkt770
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