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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 9
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pubmed:dateCreated |
2003-3-31
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pubmed:abstractText |
Cell cycle dynamics and localization of condensins--multiprotein complexes involved in late stages of mitotic chromosome condensation--were studied in Xenopus laevis XL2 cell line. Western blot analysis of synchronized cells showed that the ratio of levels of both pEg7 and XCAP-E to beta-tubulin levels remains almost constant from G1 to M phase. pEg7 and XCAP-E were localized to the mitotic chromosomes and were detected in interphase nuclei. Immunostaining for condensins and nucleolar proteins UBF, fibrillarin and B23 revealed that both XCAP-E and pEg7 are localized in the granular component of the nucleolus. Nucleolar labeling of both proteins is preserved in segregated nucleoli after 6 hours of incubation with actinomycin D (5 mg/ml), but the size of the labeled zone was significantly smaller. The data suggest a novel interphase function of condensin subunits in spatial organization of the nucleolus and/or ribosome biogenesis.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Eg7 protein, Xenopus,
http://linkedlifedata.com/resource/pubmed/chemical/Egg Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Ribosomal,
http://linkedlifedata.com/resource/pubmed/chemical/XCAP-E protein, Xenopus,
http://linkedlifedata.com/resource/pubmed/chemical/Xenopus Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/condensin complexes
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9533
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
116
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1667-78
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12665548-Adenosine Triphosphatases,
pubmed-meshheading:12665548-Animals,
pubmed-meshheading:12665548-Carrier Proteins,
pubmed-meshheading:12665548-Cell Cycle,
pubmed-meshheading:12665548-Cell Cycle Proteins,
pubmed-meshheading:12665548-Cell Line,
pubmed-meshheading:12665548-Cell Nucleolus,
pubmed-meshheading:12665548-Chromosomes,
pubmed-meshheading:12665548-DNA-Binding Proteins,
pubmed-meshheading:12665548-Egg Proteins,
pubmed-meshheading:12665548-Interphase,
pubmed-meshheading:12665548-Macromolecular Substances,
pubmed-meshheading:12665548-Microscopy, Immunoelectron,
pubmed-meshheading:12665548-Multiprotein Complexes,
pubmed-meshheading:12665548-Nuclear Proteins,
pubmed-meshheading:12665548-RNA, Ribosomal,
pubmed-meshheading:12665548-Transcription, Genetic,
pubmed-meshheading:12665548-Xenopus Proteins,
pubmed-meshheading:12665548-Xenopus laevis
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pubmed:year |
2003
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pubmed:articleTitle |
Nucleolar association of pEg7 and XCAP-E, two members of Xenopus laevis condensin complex in interphase cells.
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pubmed:affiliation |
Groupe Structure Dynamique de la Chromatine, CNRS, UMR 6061, Faculte de Medicine, 35043 Rennes, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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