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FEBS Lett. 2008 Jun 18;582(14):1997-2003. doi: 10.1016/j.febslet.2008.03.009. Epub 2008 Mar 17.

Deciphering the assembly pathway of Sm-class U snRNPs.

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Theodor-Boveri Institute at the Biocenter, Am Hubland, University of Wuerzburg, D-97074 Wuerzburg, Germany.


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.

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