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note
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The complete coding sequence of human CRM1 was amplified by polymerase chain reaction from an HPBALL cell cDNA library and cloned into the Kpn I and Xba I sites of pcDNA3 plasmid (Invitrogen).
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27
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1842286220
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note
-
35S-cysteine (Amersham). Translation products were analyzed by SDS-PAGE and autoradiography. For immunoprecipitation experiments, CRM1 was cotranslated with either wild-type IκBα or LκBα-L234. Five microliters of each TNT reaction was incubated in 40 μl of phosphate-buffered saline (PBS) containing BSA (100 μg/ml) for 30 min at room temperature before being immunoprecipitated with 2.5 μg of either anti-MYC tag or anti-SV5 tag in the presence of 20 μl of protein G-Sepharose (Pharmacia). After being washed in PBS containing 0.1% NP-40, samples were treated with Laemmli sample buffer for 2 min at 95°C and analyzed by 7% SDS-PAGE and fluorography. We obtained NES or mutated NES affinity columns by coupling biotinylated BSA (Pierce) first to sulfosuccinimidyl 4-(N-maleimidomethyl)cyclohexane-1-carboxylate (Pierce) and then to NES peptide (CIQQQLGQLTLENL) or mutated NES peptide (CIQQQAGQATAENA) (9). For each condition, 16 μg of biotinylated BSA coupled to the peptides was bound to 20 μl of streptavidin-agarose. After being washed in PBS, beads were incubated in 40 μl of PBS containing BSA (100 μg/ml), 3 μl of the TNT reaction, and peptides (2 mg/ml) for the competition experiments for 30 min at room temperature. Unbound fractions were collected and sedimented material was extensively washed in PBS before being treated with Laemmli sample buffer for 2 min at 95°C. Samples were analyzed by 7% SDS-PAGE and fluorography.
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28
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1842264731
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note
-
Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; E, Glu; G, Gly; I, Ile; L, Leu; N, Asn; Q, Gln; and T, Thr.
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note
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6 cells/ml. Fifty microliters of DNA mix (210 mM NaC;, 10 μg of specific DNA, and 30 μg of carrier DNA) was added to 200 μl of cell suspension before electroporation (950 μF, 240 V, with Gene Pulser II; Bio-Rad). Cells were subsequently cultured for 18 hours before analysis. Forty percent of cells were transfected by this protocol.
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33
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0025083331
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1842396921
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note
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For indirect immunofluorescence analysis, cells were fixed for 10 min with 2% paraformaldehyde and 0.1% glutaraldehyde and permeabilized with 0.1% Triton X-100 for 5 min. A monoclonal antibody (mAb) to MYC (9E10) was applied for 30 min followed by a 30-min incubation with fluorescein isothiocyanate-conjugated donkey anti-mouse immunoglobulin G (Jackson). Cover slips were mounted in Moviol (Hoechst, Frankfurt, Germany). Photographs corresponding to the different conditions were taken with the same setting parameters.
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35
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1842381355
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note
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Cells were treated first with 1 μg of deoxyribonuclease I before being lysed in Laemmli sample buffer containing 8 M urea. Proteins were resolved by 10% SDS-PAGE and transferred to nitrocellulose membrane. Membranes were incubated with mAb 9E10 and an mAb to hnRNP C (4F4), followed by an incubation with anti-mouse coupled to horseradish peroxidase, and finally developed with the chemiluminescence protein immunoblotting reagents (POD, Boehringer Mannheim, Germany). Quantitation of protein immunoblots was performed with the Bioprint acquisition system and Bioprofil program (Vilbert Lourmat).
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note
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We thank Novartis and particularly B. Wolff for leptomycin B; G. Dreyfuss for the anti-hnRNP C; C. Maison for helpful and stimulating discussions; and D. Louvard, J. Salamero, and R. Golsteyn for critical reading of the manuscript. Supported by grants from Action Thematique et Incitative sur Programme et Equipes-CNRS, the Association de Recherche Contre le Cancer, and the European Communities Concerted Action (project: Rocio II).
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