title: Deciphering the assembly pathway of Sm-class U snRNPs.
abstract: The assembly of the Sm-class of uridine-rich small nuclear ribonucleoproteins (U snRNPs), albeit spontaneous in vitro, has recently been shown to be dependent on the aid of a large number of assisting factors in vivo. These factors are organized in two interacting units termed survival motor neuron (SMN)- and protein arginine methyltransferase 5 (PRMT5)-complexes, respectively. While the PRMT5-complex acts early in the assembly pathway by activating common proteins of U snRNPs, the SMN-complex functions to join proteins and RNA in a highly ordered, apparently regulated manner. Here, we summarize recent progress in the understanding of this process and discuss the influence exerted by the aforementioned trans-acting factors.
authors: Theodor-Boveri Institute at the Biocenter, Am Hubland, University of Wuerzburg, D-97074 Wuerzburg, Germany.
authors: Nils
authors: N
authors: Neuenkirchen
authors: Ashwin
authors: A
authors: Chari
authors: Utz
authors: U
authors: Fischer
mesh_terms: D002467:Cell Nucleus / Q000378:metabolism*; D006801:Humans; D011496:Protein Methyltransferases / Q000378:metabolism; D011484:Protein-Arginine N-Methyltransferases; D017411:Ribonucleoproteins, Small Nuclear / Q000378:metabolism*; D017381:Spliceosomes / Q000378:metabolism*
chemical_list: D017411:Ribonucleoproteins, Small Nuclear; D011496:Protein Methyltransferases; C400529:PRMT5 protein, human; D011484:Protein-Arginine N-Methyltransferases