Deciphering the assembly pathway of Sm-class U snRNPs |
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| Authors: | Neuenkirchen Nils Chari Ashwin Fischer Utz |
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| Affiliation: | Theodor-Boveri Institute at the Biocenter, Am Hubland, University of Wuerzburg, D-97074 Wuerzburg, Germany. |
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| 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. |
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| Keywords: | snRNA, small nuclear RNA snRNP, small nuclear ribonucleoprotein SMN, survival motor neuron PRMT5, protein arginine methyltransferase 5 WD45, WD repeat domain 45 pICln, chloride conductance regulatory protein CBC, cap-binding complex PHAX, phosphorylated adaptor for RNA export CRM1, chromosome region maintenance 1 RanGTP, Ras-related nuclear protein bound to GTP NPC, nuclear pore complex Tgs1, trimethylguanosine synthetase1 NLS, nuclear localization signal SPN1, snurportin-1 Lsm proteins, like Sm protein |
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