Previous Article | Next Article ![]()
Molecular and Cellular Biology, January 1999, p. 251-260, Vol. 19, No. 1
Institut de Biologie-CHR, INSERM U463, 44093 Nantes Cedex 1, France
Received 27 May 1998/Returned for modification 17 July
1998/Accepted 23 September 1998
Some exons contain exon splicing silencers. Their activity is
frequently balanced by that of splicing enhancers, and this is
important to ensure correct relative levels of alternatively spliced
mRNAs. Using an immunoprecipitation and UV-cross-linking assay, we show
that RNA molecules containing splicing silencers from the human
immunodeficiency virus type 1 tat exon 2 or the human fibroblast growth
factor receptor 2 K-SAM exon bind to hnRNP A1 in HeLa cell nuclear
extracts better than the corresponding RNA molecule without a
silencer. Two different point mutations which abolish the K-SAM
exon splicing silencer's activity reduce hnRNP A1 binding twofold.
Recruitment of hnRNP A1 in the form of a fusion with bacteriophage MS2
coat protein to a K-SAM exon whose exon splicing silencer has been
replaced by a coat binding site efficiently represses splicing
of the exon in vivo. Recruitment of only the glycine-rich C-terminal
domain of hnRNP A1, which is capable of interactions with other
proteins, is sufficient to repress exon splicing. Our results show that
hnRNP A1 can function to repress splicing, and they suggest that at
least some exon splicing silencers could work by recruiting hnRNP A1.
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
hnRNP A1 Recruited to an Exon In Vivo Can
Function as an Exon Splicing Silencer
*
Corresponding author. Mailing address: INSERM U463,
Institut de Biologie-CHR, 9 Quai Moncousu, 44093 Nantes Cedex 1, France. Phone: (33) 02 40 08 47 50. Fax: (33) 02 40 35 66 97. E-mail: breathna{at}nantes.inserm.fr.
This article has been cited by other articles:
| J. Bacteriol. | J. Virol. | Eukaryot. Cell |
|---|
| Microbiol. Mol. Biol. Rev. | Clin. Vaccine Immunol. | All ASM Journals |
|---|