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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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| Zeitschriftentitel: | Journal of Cell Science |
|---|---|
| Personen und Körperschaften: | , , |
| In: | Journal of Cell Science, 117, 2004, 8, S. 1553-1566 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
The Company of Biologists
|
| Schlagwörter: |
| author_facet |
Zhao, Jian Jin, Shao-Bo Wieslander, Lars Zhao, Jian Jin, Shao-Bo Wieslander, Lars |
|---|---|
| author |
Zhao, Jian Jin, Shao-Bo Wieslander, Lars |
| spellingShingle |
Zhao, Jian Jin, Shao-Bo Wieslander, Lars Journal of Cell Science 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 Cell Biology |
| author_sort |
zhao, jian |
| spelling |
Zhao, Jian Jin, Shao-Bo Wieslander, Lars 1477-9137 0021-9533 The Company of Biologists Cell Biology http://dx.doi.org/10.1242/jcs.00992 <jats:p>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-β-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.</jats:p> 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 Journal of Cell Science |
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10.1242/jcs.00992 |
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Online Free |
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DE-105 DE-14 DE-Ch1 DE-L229 DE-D275 DE-Bn3 DE-Brt1 DE-Zwi2 DE-D161 DE-Gla1 DE-Zi4 DE-15 DE-Rs1 DE-Pl11 |
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The Company of Biologists, 2004 |
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The Company of Biologists, 2004 |
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49 |
| title |
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 |
| title_unstemmed |
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 |
| title_full |
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 |
| title_fullStr |
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 |
| title_full_unstemmed |
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 |
| title_short |
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 |
| title_sort |
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 |
| topic |
Cell Biology |
| url |
http://dx.doi.org/10.1242/jcs.00992 |
| publishDate |
2004 |
| physical |
1553-1566 |
| description |
<jats:p>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-β-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.</jats:p> |
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| author | Zhao, Jian, Jin, Shao-Bo, Wieslander, Lars |
| author_facet | Zhao, Jian, Jin, Shao-Bo, Wieslander, Lars, Zhao, Jian, Jin, Shao-Bo, Wieslander, Lars |
| author_sort | zhao, jian |
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| container_start_page | 1553 |
| container_title | Journal of Cell Science |
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| description | <jats:p>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-β-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.</jats:p> |
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| imprint | The Company of Biologists, 2004 |
| imprint_str_mv | The Company of Biologists, 2004 |
| institution | DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Rs1, DE-Pl11 |
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| physical | 1553-1566 |
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| series | Journal of Cell Science |
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| spelling | Zhao, Jian Jin, Shao-Bo Wieslander, Lars 1477-9137 0021-9533 The Company of Biologists Cell Biology http://dx.doi.org/10.1242/jcs.00992 <jats:p>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-β-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.</jats:p> 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 Journal of Cell Science |
| spellingShingle | Zhao, Jian, Jin, Shao-Bo, Wieslander, Lars, Journal of Cell Science, 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, Cell Biology |
| title | 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 |
| title_full | 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 |
| title_fullStr | 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 |
| title_full_unstemmed | 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 |
| title_short | 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 |
| title_sort | 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 |
| title_unstemmed | 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 |
| topic | Cell Biology |
| url | http://dx.doi.org/10.1242/jcs.00992 |