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Deciphering the assembly pathway of Sm‐class U snRNPs

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Chari,  A.
Research Group of Structural Biochemistry and Mechanisms, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

Neuenkirchen, N., Chari, A., & Fischer, U. (2008). Deciphering the assembly pathway of Sm‐class U snRNPs. FEBS Letters, 582(14), 1997-2003. doi:10.1016/j.febslet.2008.03.009.


Cite as: http://hdl.handle.net/21.11116/0000-0008-0FDC-1
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.