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dc.contributor.authorSmith, Kelly P.
dc.contributor.authorByron, Meg
dc.contributor.authorClemson, Christine M.
dc.contributor.authorLawrence, Jeanne B.
dc.date2022-08-11T08:08:48.000
dc.date.accessioned2022-08-23T16:08:56Z
dc.date.available2022-08-23T16:08:56Z
dc.date.issued2004-12-24
dc.date.submitted2009-01-12
dc.identifier.citationChromosoma. 2004 Dec;113(6):324-35. Epub 2004 Nov 20. <a href="http://dx.doi.org/10.1007/s00412-004-0325-1">Link to article on publisher's site</a>
dc.identifier.issn0009-5915 (Print)
dc.identifier.doi10.1007/s00412-004-0325-1
dc.identifier.pmid15616869
dc.identifier.urihttp://hdl.handle.net/20.500.14038/32569
dc.description.abstractThe inactive X chromosome (Xi) forms a heterochromatic structure in the nucleus that is known to have several modifications to specific histones involving acetylation or methylation. Using three different antibodies in four different cell lines, we demonstrate that the Xi in human and mouse cells is highly enriched in ubiquitinated protein(s), much of which is polyubiquitinated. This ubiquitination appears specific for the Xi as it was not observed for centromeres or other regions of heterochromatin. Results using an antibody specific to ubiquitinated H2A provide a clear link between H2A ubiquitination and gene repression, as visualized across an entire inactive chromosome. Interestingly, the ubiquitination of the chromosome persists into mitosis and can be seen in a reproducible banded pattern. This pattern matches that of Xist RNA which forms bands as it detaches from the mitotic X chromosome. Both ubiquitination and Xist RNA appear enriched in gene dense regions and depleted in gene poor bands, but do not correlate with L1 LINE elements which have been suggested as key to X-inactivation. These results provide evidence that ubiquitination along with Xist RNA plays an important role in the formation of facultative heterochromatin during X-inactivation.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=15616869&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1007/s00412-004-0325-1
dc.subjectAnimals; Antibodies, Monoclonal; Cell Line; Chromosomes, Human, X; *Dosage Compensation, Genetic; Down-Regulation; Gene Expression; Histones; Humans; Mice; Mitosis; RNA, Untranslated; Sex Chromatin; Ubiquitins; X Chromosome
dc.subjectCell Biology
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleUbiquitinated proteins including uH2A on the human and mouse inactive X chromosome: enrichment in gene rich bands
dc.typeJournal Article
dc.source.journaltitleChromosoma
dc.source.volume113
dc.source.issue6
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/1132
dc.identifier.contextkey692125
html.description.abstract<p>The inactive X chromosome (Xi) forms a heterochromatic structure in the nucleus that is known to have several modifications to specific histones involving acetylation or methylation. Using three different antibodies in four different cell lines, we demonstrate that the Xi in human and mouse cells is highly enriched in ubiquitinated protein(s), much of which is polyubiquitinated. This ubiquitination appears specific for the Xi as it was not observed for centromeres or other regions of heterochromatin. Results using an antibody specific to ubiquitinated H2A provide a clear link between H2A ubiquitination and gene repression, as visualized across an entire inactive chromosome. Interestingly, the ubiquitination of the chromosome persists into mitosis and can be seen in a reproducible banded pattern. This pattern matches that of Xist RNA which forms bands as it detaches from the mitotic X chromosome. Both ubiquitination and Xist RNA appear enriched in gene dense regions and depleted in gene poor bands, but do not correlate with L1 LINE elements which have been suggested as key to X-inactivation. These results provide evidence that ubiquitination along with Xist RNA plays an important role in the formation of facultative heterochromatin during X-inactivation.</p>
dc.identifier.submissionpathgsbs_sp/1132
dc.contributor.departmentDepartment of Cell Biology
dc.source.pages324-35
dc.contributor.studentChristine Clemson


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