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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 8
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pubmed:dateCreated |
2004-3-15
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pubmed:abstractText |
Messenger RNA is formed from precursors known as pre-mRNA. These precursors associate with proteins to form pre-mRNA-protein (pre-mRNP) complexes. Processing machines cap, splice and polyadenylate the pre-mRNP and in this way build the mRNP. These processing machines also affect the export of the mRNP complexes from the nucleus to the cytoplasm. Export to the cytoplasm takes place through a structure in the nuclear membrane called the nuclear pore complex (NPC). Export involves adapter proteins in the mRNP and receptor proteins that bind to the adapter proteins and to components of the NPC. We show that the export receptor chromosomal region maintenance protein 1 (CRM1), belonging to a family of proteins known as importin-beta-like proteins, binds to gene-specific Balbiani ring (BR) pre-mRNP while transcription takes place. We also show that the GTPase known as Ran binds to BR pre-mRNP, and that it binds mainly in the interchromatin. However, we also show using leptomycin B treatment that a NES-CRM1-RanGTP complex is not essential for export, even though both CRM1 and Ran accompany the BR mRNP through the NPC. Our results therefore suggest that several export receptors associate with BR mRNP and that these receptors have redundant functions in the nuclear export of BR mRNP.
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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/Fatty Acids, Unsaturated,
http://linkedlifedata.com/resource/pubmed/chemical/Karyopherins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/exportin 1 protein,
http://linkedlifedata.com/resource/pubmed/chemical/leptomycin B,
http://linkedlifedata.com/resource/pubmed/chemical/messenger ribonucleoprotein,
http://linkedlifedata.com/resource/pubmed/chemical/ran GTP-Binding Protein
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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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 |
15
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pubmed:volume |
117
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1553-66
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15020682-Animals,
pubmed-meshheading:15020682-Blotting, Western,
pubmed-meshheading:15020682-Cell Nucleus,
pubmed-meshheading:15020682-Cells, Cultured,
pubmed-meshheading:15020682-Chironomidae,
pubmed-meshheading:15020682-Chromosomes,
pubmed-meshheading:15020682-Cytoplasm,
pubmed-meshheading:15020682-Escherichia coli,
pubmed-meshheading:15020682-Fatty Acids, Unsaturated,
pubmed-meshheading:15020682-Gene Expression,
pubmed-meshheading:15020682-Karyopherins,
pubmed-meshheading:15020682-Nuclear Pore,
pubmed-meshheading:15020682-Precipitin Tests,
pubmed-meshheading:15020682-Protein Binding,
pubmed-meshheading:15020682-RNA Precursors,
pubmed-meshheading:15020682-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:15020682-Ribonucleoproteins,
pubmed-meshheading:15020682-Salivary Glands,
pubmed-meshheading:15020682-Transcription, Genetic,
pubmed-meshheading:15020682-ran GTP-Binding Protein
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pubmed:year |
2004
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pubmed:articleTitle |
CRM1 and Ran are present but a NES-CRM1-RanGTP complex is not required in Balbiani ring mRNP particles from the gene to the cytoplasm.
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pubmed:affiliation |
Department of Molecular Biology and Functional Genomics, Stockholm University, SE-106 91 Stockholm, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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