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          Institute: MPI für biophysikalische Chemie     Collection: Zelluläre Biochemie (Prof. Reinhard Lührmann)     Display Documents

ID: 16911.0, MPI für biophysikalische Chemie / Zelluläre Biochemie (Prof. Reinhard Lührmann)
Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln
Authors:Meister, G.; Eggert, C.; Buehler, D.; Brahms, H.; Kambach, C.; Fischer, U.
Date of Publication (YYYY-MM-DD):2001-12-11
Title of Journal:Current Biology
Issue / Number:24
Start Page:1990
End Page:1994
Review Status:Peer-review
Audience:Not Specified
Abstract / Description:Seven Sm proteins, termed B/B', D1, D2F D3, E, F, and G, assemble in an ordered manner onto U snRNAs to form the Sm core of the spliceosomal: snRNPs U1, U2, U4/U6, and U5 [1-4]. The survival of motor neuron (SMN) protein binds to Sm proteins and mediates in the context of a macromolecular (SMN-) complex the assembly of the Sm core [5-9]. Binding of SMN to Sm proteins is enhanced by modification of specific arginine residues in the Sm proteins D1 and D3 to symmetrical dimethylarginines (sDMAs), suggesting that assembly might be regulated at the posttranslational level [10-12]. Here we provide evidence that the previously described pICIn-complex [13], consisting of Sm proteins, the methyltransferase PRMT5, pICIn, and two novel factors, catalyzes the sDMA modification of Sm proteins. In vitro studies further revealed that the pICIn complex inhibits the spontaneous assembly of Sm proteins onto a U snRNA. This effect is mediated by pICIn via its binding to the Sm fold, of Sm proteins, thereby preventing specific interactions between Sm proteins required for the formation of the Sm core. Our data suggest that the pICIn complex regulates an early step in the assembly of U snRNPs, possibly the transfer of Sm proteins to the SMN-complex.
Comment of the Author/Creator:Date: 2001, DEC 11
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für biophysikalische Chemie/Abt. Reinhard Lührmann / 100
External Affiliations:Max Planck Inst Biochem, Klopferspitz 18A, D-82152 Martinsried,; Germany; Max Planck Inst Biochem, D-82152 Martinsried, Germany; Paul Scherrer Inst, CH-5232 Villigen, Switzerland
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