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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Dickmanns, Achim Huber, Jochen Lührmann, Reinhard |
| Description | Author Affiliation: Huber J ( Department of Cellular Biochemistry, Max Planck Institute of Biophysical Chemistry, D-37077 Göttingen, Germany.) |
| Abstract | The nuclear localization signal (NLS) of spliceosomal U snRNPs is composed of the U snRNA's 2,2,7-trimethyl-guanosine $(m_{3}G)-cap$ and the Sm core domain. The $m_{3}G-cap$ is specifically bound by snurportin1, which contains an $NH_{2}-terminal$ importin-β binding (IBB) domain and a COOH-terminal $m_{3}G-cap–binding$ region that bears no structural similarity to known import adaptors like importin-α (impα). Here, we show that recombinant snurportin1 and importin-β (impβ) are not only necessary, but also sufficient for U1 snRNP transport to the nuclei of digitonin-permeabilized HeLa cells. In contrast to impα–dependent import, single rounds of U1 snRNP import, mediated by the nuclear import receptor complex snurportin1–impβ, did not require Ran and energy. The same Ran- and energy-independent import was even observed for U5 snRNP, which has a molecular weight of more than one million. Interestingly, in the presence of impβ and a snurportin1 mutant containing an impα IBB domain $(IBB_{impα}),$ nuclear U1 snRNP import was Ran dependent. Furthermore, β-galactosidase (βGal) containing a snurportin1 IBB domain, but not $IBB_{impα}-βGal,$ was imported into the nucleus in a Ran-independent manner. Our results suggest that the nature of the IBB domain modulates the strength and/or site of interaction of impβ with nucleoporins of the nuclear pore complex, and thus whether or not Ran is required to dissociate these interactions. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 3 |
| Volume Number | 156 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 2002-02-04 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Active Transport, Cell Nucleus Physiology Nuclear Pore Metabolism Receptors, Cytoplasmic And Nuclear Ribonucleoprotein, U1 Small Nuclear Spliceosomes Beta Karyopherins Ran GTP-Binding Protein Adenosine Triphosphate Genetics Energy Metabolism Genes, Reporter Guanosine Triphosphate HeLa Cells In Vitro Techniques Protein Structure, Tertiary RNA Cap-Binding Proteins Recombinant Fusion Proteins Beta-Galactosidase Research Support, Non-U.S. Gov't Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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