Xenbase is experiencing difficulties due to technical problems with the University of Calgary IT infrastructure and may go temporarily offline.

Click on this message to dismiss it.
Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
Nat Cell Biol. November 1, 2001; 3 (11): 945-9.

A multiprotein complex mediates the ATP-dependent assembly of spliceosomal U snRNPs.

Meister G , B├╝hler 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.

Genes referenced: gemin2

My Xenbase: [ Log-in / Register ]
version: [3.11.2]

Major funding for Xenbase is provided by the National Institute of Child Health and Human Development, grant P41 HD064556