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Journal Articles EMBO Reports Year : 2009

Human U1 snRNA forms a new chromatin-associated snRNP with TAF15.

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Abstract

The U1 small nuclear RNA (snRNA)--in the form of the U1 spliceosomal Sm small nuclear ribonucleoprotein particle (snRNP) that contains seven Sm and three U1-specific RNP proteins-has a crucial function in the recognition and removal of pre-messenger RNA introns. Here, we show that a fraction of human U1 snRNA specifically associates with the nuclear RNA-binding protein TBP-associated factor 15 (TAF15). We show that none of the known protein components of the spliceosomal U1-Sm snRNP interacts with the newly identified U1-TAF15 snRNP. In addition, the U1-TAF15 snRNP tightly associates with chromatin in an RNA-dependent manner and accumulates in nucleolar caps upon transcriptional inhibition. The Sm-binding motif of U1 snRNA is essential for the biogenesis of both U1-Sm and U1-TAF15 snRNPs, suggesting that the U1-TAF15 particle is produced by remodelling of the U1-Sm snRNP. A demonstration that human U1 snRNA forms at least two structurally distinct snRNPs supports the idea that the U1 snRNA has many nuclear functions.

Dates and versions

inserm-00384441 , version 1 (15-05-2009)

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Laure Jobert, Natalia Pinzón, Elodie van Herreweghe, Beáta E. Jády, Apostolia Guialis, et al.. Human U1 snRNA forms a new chromatin-associated snRNP with TAF15.. EMBO Reports, 2009, 10 (5), pp.494-500. ⟨10.1038/embor.2009.24⟩. ⟨inserm-00384441⟩
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