rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
3
|
pubmed:dateCreated |
2003-10-2
|
pubmed:abstractText |
The 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.
|
pubmed:language |
rus
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:issn |
0041-3771
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
45
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
290-7
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:14520886-Animals,
pubmed-meshheading:14520886-Carrier Proteins,
pubmed-meshheading:14520886-Cell Line,
pubmed-meshheading:14520886-Cell Nucleus,
pubmed-meshheading:14520886-Interphase,
pubmed-meshheading:14520886-Microscopy, Electron,
pubmed-meshheading:14520886-Nuclear Proteins,
pubmed-meshheading:14520886-RNA, Ribosomal,
pubmed-meshheading:14520886-RNA Processing, Post-Transcriptional,
pubmed-meshheading:14520886-Ribonucleoproteins,
pubmed-meshheading:14520886-Transcription, Genetic,
pubmed-meshheading:14520886-Transcription Factors,
pubmed-meshheading:14520886-Xenopus Proteins,
pubmed-meshheading:14520886-Xenopus laevis
|
pubmed:year |
2003
|
pubmed:articleTitle |
[Intracellular localization of XCAP-E protein in XL2 (Xenopus laevis) cells under normal conditions and during inhibition of pRNA transcription and processing].
|
pubmed:affiliation |
Research Institute of Physico-Chemical Biology, Moscow State University, Institute of Gene Biology RAS, Moscow. al_mira@rambler.ru
|
pubmed:publicationType |
Journal Article,
English Abstract
|