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As described previously 10 , the RK3 minigene Fig. Transfection of epithelial SVK14 cells with RK3 leads to preferential splicing of the K-SAM exon, while transfection of EBNA cells leads to preferential splicing of the BEK exon.

Skipping of both exons is also observed at a low level. Cotransfection of EBNA cells with RK3 and pcoat a bacteriophage MS2 coat protein expression vector resulted in BEK exon splicing Fig.

For RK3 and derivatives, two probes were used to identify RT-PCR products. The C1C2 probe detects all products, while the K-SAM probe detects only products containing the K-SAM exon.

Cotransfection of RK3 with pTIA-1 resulted in splicing of the K-SAM exon to the BEK exon Fig. Importantly, cotransfection of RK3 with the hnRNP C1 expression vector did not detectably activate K-SAM exon splicing lanes 3 , suggesting that the TIA-1 effect on the K-SAM exon cannot be reproduced by just any U-rich sequence binding protein.

RK20 Fig. Cotransfection of RK20 with pTIA-1 did not lead to K-SAM exon splicing, as RT-PCR products of type C1BC2 Fig.

TIA-1 activation of K-SAM exon splicing is thus IAS1 dependent. Note that, in the absence of IAS1, TIA-1 activates splicing of C1 to C2 somewhat Fig.

Schematic representations of FGFR-2 minigenes. The parent minigene RK3 is shown, with the Rous sarcoma virus long terminal repeat promoter RSV , the alternative exons K-SAM and BEK, the upstream and downstream constitutive exons C1 and C2, and the bovine growth hormone polyadenylation sequence BGH.

Locations of primers P3 and P4 used for RT-PCR are marked. The U-rich intron-activating sequence IAS1 is identified. RK20 is similar to RK3, except for the replacement of IAS1 with a random sequence.

RK98 was derived from RK97 by replacing IAS1 with the random sequence described in the text. RK-MS2 is derived from RK3 by replacing IAS1 and some downstream sequences with bacteriophage MS2 coat binding sites MS2.

In addition, the BEK exon is deleted. TIA-1 activation of the K-SAM exon requires IAS1. Cells were cotransfected with minigenes and expression vectors for bacteriophage MS2 coat protein, TIA-1, or hnRNP C1 as shown.

RT-PCR was carried out on transfected cell RNA using primers P3 and P4 shown in Fig. Hybridization was performed first to a probe corresponding to the K-SAM exon B and D , and then the same blot was dehybridized and rehybridized to a probe made up of exons C1 and C2 A and C.

RT-PCR products are identified using names corresponding to structures shown in panel E. TIA-1 can activate K-SAM exon splicing not only to the BEK exon but also to the C2 exon.

In RK97 Fig. Cotransfection of RK97 with pcoat in EBNA cells results mainly in skipping of the K-SAM exon. The major RT-PCR product obtained Fig.

Cotransfection of RK97 with pTIA-1 leads to a marked increase of K-SAM exon splicing, as evidenced by an increase in the levels of the C1SC2 product Fig.

Once again, this activation of K-SAM splicing is IAS1 dependent, as cotransfection of pTIA-1 with RK98, a version of RK97 in which IAS1 has been replaced with the random sequence Fig.

In RK-MS2 Fig. Proteins can thus be recruited to RK-MS2 pre-mRNA downstream from the K-SAM exon as fusions with coat protein.

When RK-MS2 is transfected together with the empty expression vector pCI-neo or pcoat, the K-SAM exon is skipped. RT-PCR products detected with the C1C2 probe Fig.

This result is expected, as IAS1 is required for efficient K-SAM exon splicing. Cotransfection of pTIA-1 with RK-MS2 does not detectably induce K-SAM exon inclusion: note that none of the RT-PCR products detected with the C1C2 probe Fig.

However, when RK-MS2 is cotransfected with an expression vector for a TIA-1—coat fusion protein, some inclusion of the K-SAM exon is induced: RT-PCR products which hybridize to the K-SAM probe and correspond to C1SC2 can be detected Fig.

No activation of K-SAM exon splicing was observed when RK-MS2 was cotransfected with expression vectors for hnRNP C1-coat fusions Fig.

Cells were cotransfected with minigenes and the empty expression vector pCI-neo or expression vectors for bacteriophage MS2 coat protein or TIA-1 or the following fusions with coat protein: TIA-1—coat fusion TIA-coat , hnRNP C1-coat fusion C1-coat , and hnRNP A1-coat fusion A1-coat.

Hybridization was performed first to a probe corresponding to the K-SAM exon B and D , followed by dehybridization and rehybridization to a probe made up of exons C1 and C2 A and C.

RT-PCR products are identified using names corresponding to structures shown in Fig. The K-SAM exon inclusion induced by TIA-coat with RK-MS2 pre-mRNA is less than that induced by TIA-1 with pre-mRNAs containing IAS1 compare Fig.

The TIA-coat fusion bound to the MS2 operator may be presented to the splicing apparatus suboptimally compared to TIA-1 in its natural position.

Activation by the TIA-coat fusion is, as expected, position dependent. In RK99 Fig. Note that RK99 does not contain IAS1, which has been replaced with the random sequence of RK When RK99 is transfected together with the TIA-coat expression vector, no activation of K-SAM exon splicing is observed Fig.

In fact, TIA-coat expression now represses K-SAM exon splicing compare lanes 1 and 2. To test whether TIA-1 can influence alternative splicing of other exons in vivo, we used several minigenes reflecting well-documented cases of alternative exon splicing.

Minigenes were cotransfected into cells with different expression vectors, and splicing patterns were investigated by RT-PCR analysis of transfected cell RNA using minigene-specific primers.

Normally, splicing of preprotachykinin pre-mRNA involves preferential skipping of optional exon 4 23 , Effects of TIA-1 and hnRNP C1 on splicing in vivo.

A The preprotachykinin minigene was cotransfected into SVK14 cells with pCI-neo lane 1 , pTIA-1 lane 2 , or phnRNP C1 lane 3.

RT-PCR was carried out on transfected cell RNA using primers P1 and P2, and products were subjected to Southern analysis with hybridization to a probe made up of exons 2 to 5.

B A hybrid FGFR-2—CD44 minigene was cotransfected into EBNA cells with pCI-neo lane 1 , pTIA-1 lane 2 , or phnRNP C1 lane 3.

RT-PCR was carried out on transfected cell RNA using primers P3 and P4 as marked, and products were subjected to Southern analysis with hybridization to a probe made up of exons C1 and C2 of the FGFR-2 gene.

The 6. On the minigene map, the three major splicing events seen in EBNA cells transfected with the minigene and pCI-neo are illustrated.

The corresponding RT-PCR products are illustrated below the map. RSV, Rous sarcoma virus long terminal repeat; BGH, bovine growth hormone polyadenylation signal.

Radioactivities present in bands were determined by phosphorimager and used to calculate splicing percentages. Exons v8, v9, and v10 of the CD44 gene's pre-mRNA are spliced to generate mRNA for the epithelial cell form of CD44 9.

A minigene was made in which these exons and their flanking introns were placed between two constitutively spliced exons, C1 and C2, of the human FGFR-2 gene Fig.

When this minigene was transfected into the epithelial cell line SVK14, exons v8, v9, and v10 were efficiently spliced to the flanking exons C1 and C2 data not shown.

However, when the minigene was transfected into EBNA cells together with the control vector pCI-neo, RT-PCR analysis revealed a number of products Fig.

The identity of some of these products was investigated by hybridization to a probe composed of v8, v9, and v10 sequences and by sequencing of subcloned fragments data not shown.

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