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pubmed-article:14520886pubmed:dateCreated2003-10-2lld:pubmed
pubmed-article:14520886pubmed:abstractTextThe interaction of condensin subunit XCAP-E with various nucleolar subcompartments in XL2 cells was studied. In the interphase cells, XCAP-E was associated with a granular component of nucleoli (as shown by double staining with antibodies against B23) and with small nucleolus-like structures in the nucleoplasm. Inhibition of transcription by actinomycin D does not disrupt interaction of XCAP-E with the granular compartment of segregated nucleoli. Treatment with DRB 5,6-dichloro-1 beta-ribofuranozide-benzimidazole causes disintegration of nucleolar fibrillar complexes, but does not affect nucleolar localization of XCAP-E. The data suggest that nucleolar association of XCAP-E is independent on the functional state of the nucleolus, and imply a possible role of this protein in rRNA processing and pre-fibosome assembly.lld:pubmed
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pubmed-article:14520886pubmed:volume45lld:pubmed
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pubmed-article:14520886pubmed:pagination290-7lld:pubmed
pubmed-article:14520886pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:14520886pubmed:year2003lld:pubmed
pubmed-article:14520886pubmed:articleTitle[Intracellular localization of XCAP-E protein in XL2 (Xenopus laevis) cells under normal conditions and during inhibition of pRNA transcription and processing].lld:pubmed
pubmed-article:14520886pubmed:affiliationResearch Institute of Physico-Chemical Biology, Moscow State University, Institute of Gene Biology RAS, Moscow. al_mira@rambler.rulld:pubmed
pubmed-article:14520886pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:14520886pubmed:publicationTypeEnglish Abstractlld:pubmed