A multiprotein complex mediates the ATP-dependent assembly of spliceosomal U snRNPs
Author: ["Gunter Meister","Dirk Bühler","Ramesh Pillai","Friedrich Lottspeich","Utz Fischer"]
Publication: Nature Cell Biology
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Abstract
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.
Cite this article
Meister, G., Bühler, D., Pillai, R. et al. A multiprotein complex mediates the ATP-dependent assembly of spliceosomal U snRNPs. Nat Cell Biol 3, 945–949 (2001). https://doi.org/10.1038/ncb1101-945
