Journal
EMBO REPORTS
Volume 10, Issue 5, Pages 494-500Publisher
WILEY
DOI: 10.1038/embor.2009.24
Keywords
TAF(II)68; non-coding RNA; U1-70K
Categories
Funding
- Ministere de l'Education Nationale
- Recherche et de la Technologie (MERT)
- Association pour la Recherche sur le Cancer (ARC)
- Centre National de la Recherche Scientifique (CNRS)
- Institut National de la Sante et de la Recherche Medicale (INSERM)
- Association for International Cancer Research (AICR) [03-084, 09-0258]
- Universite Paul Sabatier, Ligue Nationale Contre le Cancer
- Fondation pour la Recherche Medicale en France (FRM)
- Agence Nationale de la recherche [(ANR) (05-BLAN-0318-01)]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [0914534] Funding Source: National Science Foundation
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0746886] Funding Source: National Science Foundation
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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.
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