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Tia Carrere was born Althea Rae Janairo in Honolulu, Hawaii. While attending Sacred Hearts Academy, Tia was discovered in a Waikiki grocery store and landed the female lead in the film Aloha Summer.

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Teri Polo was born in Dover, Delaware, to Jane Gentry and Vincent Polo, a stereo systems designer. Her ancestry includes Italian from her paternal grandfather , German, and English.

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Select a wall color and floor material. If IAS1 is replaced with a bacteriophage MS2 operator, splicing of the K-SAM exon can no longer be activated by TIA TIA-1 is distantly related to the yeast U1 snRNP protein Nam8p, and the functional similarities between the two proteins are discussed.

Many eucaryotic genes are made up of exons and introns They are transcribed into pre-mRNAs, from which the intron sequences are removed by splicing.

Exons to be included in mRNA must be identified as such. Exon splicing can be controlled, and several sequences which participate in the control of tissue-specific or developmentally controlled alternative splicing events have been described for a review, see reference These sequences are particularly interesting to study, as they may yield information on both splicing activation mechanisms and tissue-specific control mechanisms of gene expression.

We have been studying fibroblast growth factor receptor 2 FGFR-2 pre-mRNA splicing for this reason. FGFR-2 alternative exons K-SAM and BEK are spliced in a tissue-specific, mutually exclusive manner, and the two types of FGFR-2 obtained bind different subsets of FGF family members The K-SAM exon is under complex control.

It has weak splice sites, and it contains an exon splicing silencer ESS which functions by recruiting hnRNP A1 To overcome the activity of this silencer, at least three activating sequences in the downstream intron are required 6 , 10 , Del Gatto-Konczak, unpublished data , the K-SAM exon is very poorly spliced, unless the ESS is inactivated also.

IAS1 and the ESS are thus major determinants of K-SAM exon splicing. However, neither element may be directly responsible for the tissue-specific splicing of the K-SAM exon.

Both elements can control splicing of heterologous exons in cells, and we have not detected any difference in their activities between cells which splice the K-SAM exon and cells which do not reference 11 and our unpublished data.

Searching for the activator based on its ability to bind IAS1 has not proved easy, as many nuclear proteins bind U-rich sequences, including U2AF 52 , polypyrimidine tract-binding protein PTB 18 , or hnRNP C Recent work on splicing in Saccharomyces cerevisiae has suggested a different approach, however.

Yeast U1 snRNP is considerably more complex than mammalian U1 snRNP 21 , and several yeast U1 snRNP proteins have no known metazoan counterpart. One such protein is Nam8p.

Its activity is optimal when these sequences are U rich 39 , The known mammalian proteins most closely related to Nam8p are a pair of very similar proteins called TIA-1 47 and the related protein TIAR TIA-1 was originally believed to be a precursor to a cytotoxic T-lymphocyte granule protein.

However, it is now known that this is not the case TIA-1 and TIAR are widely expressed RNA-binding proteins 3 , However, under normal conditions, the proteins are in general located mainly in the nucleus 28 ; C.

Le Guiner, unpublished data. Predominantly nuclear localization has also been described previously for UBP1, a recently characterized TIA-1—TIAR relative in plants, which enhances splicing of suboptimal introns and also protects mRNAs from exonucleolytic degradation Like Nam8p, TIA-1 and TIAR are composed of an N-terminal domain containing three RNA recognition motifs, linked to a C-terminal domain 27 , Both TIA-1 and TIAR bind to RNA, with the preferred binding sequence being U rich These observations encouraged us to test if TIA-1 is able to activate splicing of exons linked to a U-rich sequence like IAS1.

We discuss the functional similarities between TIA-1 and Nam8p. A mouse TIA-1 cDNA clone was obtained as an I. It was used to make pTIA-1, an expression vector for an N-terminal FLAG-tagged TIA-1, and pTIA-coat, an expression vector for an N-terminal FLAG-tagged TIA-1—coat fusion.

The coat expression vector pcoat or pCI-MS2 and the hnRNP A1-coat fusion vector have been described elsewhere The entire coding sequence of hnRNP C1 was introduced into the Stu I site of pCI-MS2-NLS-FLAG 13 to make an expression vector for an N-terminal FLAG-tagged hnRNP C1-coat fusion in which coat sequences are C terminal.

The hnRNP C1 expression vector phnRNP C1 was obtained from it by eliminating coat sequences by Bam HI digestion and religation.

The CD44 minigene was obtained by cloning a 6. HeLa nuclear extract and cytoplasmic S extract were prepared as described previously For preparation of whole-cell extracts WCE from EBNA cells, cells resuspended in lysis buffer 20 mM Tris-HCl [pH 7.

The supernatant WCE was dialyzed against buffer D for 5 h. Capped 32 P-labeled pre-mRNA substrates were made by runoff in vitro transcription with SP6 RNA polymerase as described in reference 8.

Splicing of the E1A-derived transcripts was performed under a variety of conditions as indicated in the figure legends.

UV cross-linking was performed as described previously 7 with minor modifications. Dreyfuss was added. Total SR proteins from HeLa cells were purified as described in reference To produce recombinant TIA-1 and hnRNP C1 in E.

Resulting plasmids were used for production of six-His-tagged proteins. They were expressed and purified under nondenaturing conditions as recommended by the manufacturer and dialyzed against buffer D for 1 h.

Transfection of SVK14 46 and EBNA cells Invitrogen was performed as described previously 10 , Forty-eight hours later, RNA was harvested and analyzed by reverse transcription-PCR RT-PCR using reporter-specific primers.

Twenty cycles of amplification were used so as to remain in the range of exponential amplification.

Experiments were carried out at least in triplicate, and representative results are shown here. Can IAS1 replace S4 in this system? Various pre-mRNA substrates Fig.

As expected from previous work 17 , splicing Fig. When S4 was replaced with IAS1 IAS1 down , Fig. In the IAS1 down pre-mRNA, IAS1 lies 43 nucleotides downstream of the exon 6A-intron junction.

Del Gatto-Konczak, unpublished data. A further pre-mRNA was made IAS1 up , Fig. Splicing of IAS1 up was at least as efficient as splicing of substrates containing S4 or the purine-rich sequence compare lanes 2, 3, and 4, Fig.

Pre-mRNA RAN Fig. Splicing of pre-mRNA RAN was significantly less efficient than splicing of substrate IAS1 up Fig. IAS1 activates splicing of a heterologous tropomyosin exon.

A Schematic representations of pre-mRNAs used for in vitro splicing. In Tropo 6A-7 pre-mRNA, exons 6A and 7 are separated by a nucleotide intron including the S4 activating sequence.

In 6A-P3AS-7 and IAS1 down , S4 has been replaced with a purine-rich sequence and with IAS1, respectively.

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