학술논문

Cooperative binding of TIA-1 and U1 snRNP in K-SAM exon splicing activation
Document Type
Author abstract
Source
Biochemical and Biophysical Research Communications. July 13, 2007, Vol. 358 Issue 4, p1065, 6 p.
Subject
Language
English
ISSN
0006-291X
Abstract
To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.bbrc.2007.05.050 Byline: Marie-Claude Gesnel, Sandrine Theoleyre, Fabienne Del Gatto-Konczak, Richard Breathnach Keywords: RNA; Alternative splicing; U1 snRNP; U1C; TIA-1; Fibroblast growth factor receptor; U-rich sequence Abstract: In 293 cells, splicing of the human fibroblast growth factor receptor-2 K-SAM alternative exon is inefficient, but can be made efficient by provoking TIA-1 binding to the U-rich IAS1 sequence downstream from the exon's 5' splice site. We show here that TIA-1 domains known to interact with U1 snRNP and to recruit it to 5' splice sites in vitro are required for TIA-1 activation of K-SAM exon splicing in vivo. We further show that tethering downstream from the K-SAM exon a fusion between the U1 snRNP component U1C and the bacteriophage MS2 coat protein provokes IAS1-dependent exon splicing, and present evidence that the fusion functions after its incorporation into U1 snRNP. Our in vivo data, taken together with previous in vitro results, show that K-SAM splicing activation involves cooperative binding of TIA-1 and U1 snRNP to the exon's 5' splice site region. Author Affiliation: INSERM, U601, Institut de Biologie -- CHR, 9 quai Moncousu, 44093 Nantes Cedex 1, France Faculte des Sciences, Universite de Nantes, Nantes, France Article History: Received 25 April 2007