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Human U1 snRNA forms a new chromatin‐associated snRNP with TAF15
Author(s) -
Jobert Laure,
Pinzón Natalia,
Van Herreweghe Elodie,
Jády Beáta E,
Guialis Apostolia,
Kiss Tamás,
Tora László
Publication year - 2009
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/embor.2009.24
Subject(s) - snrnp , small nuclear rna , prp24 , small nuclear ribonucleoprotein , biology , ribonucleoprotein , spliceosome , rna splicing , rna , genetics , microbiology and biotechnology , rna binding protein , cajal body , non coding rna , gene
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.