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Nat Cell Biol 2001 Nov 01;311:945-9. doi: 10.1038/ncb1101-945.
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A multiprotein complex mediates the ATP-dependent assembly of spliceosomal U snRNPs.

Meister G , Bühler D , Pillai R , Lottspeich F , Fischer U .

The spliceosomal snRNPs U1, U2, U4 and U5 contain a common RNP structure termed the Sm core that is formed by the binding of Sm proteins onto the U snRNA. Although isolated Sm proteins assemble spontaneously onto U snRNAs in vitro, there is increasing evidence that SMN and its interactor Gemin2 are involved in this process in vivo. Here, we describe a cell-free assay system for the assembly of U snRNPs that closely reproduces in vivo conditions. Using this system, we show that assembly of U1 snRNP depends on ATP. Immunodepletion of SMN-Gemin2 from the extract abolished assembly even though the extract contained high levels of Sm proteins. An affinity-purified macromolecular SMN complex consisting of 16 components including all Sm proteins restored assembly in the immunodepleted extract. These data provide the first direct evidence that a complex containing SMN and Gemin2 mediates the active assembly of spliceosomal U snRNPs.

PubMed ID: 11715014
Article link: Nat Cell Biol

Species referenced: Xenopus laevis
Genes referenced: gemin2 smn1