Reconstitution of the human U snRNP assembly machinery reveals stepwise Sm protein organization

• Published in: The EMBO journal Vol. 34; no. 14; pp. 1925 - 1941
• Main Authors: Neuenkirchen, Nils, Englbrecht, Clemens, Ohmer, Jürgen, Ziegenhals, Thomas, Chari, Ashwin, Fischer, Utz
• Format: Journal Article
• Language: English
• Published: London Blackwell Publishing Ltd 14.07.2015; Nature Publishing Group UK; Springer Nature B.V; John Wiley & Sons, Ltd
• Subjects: Animals; assembly; DEAD Box Protein 20 - genetics; DEAD Box Protein 20 - metabolism; EMBO36; Humans; Minor Histocompatibility Antigens; Mode of action; Molecular biology; Muscular Atrophy, Spinal - genetics; Mutation; pICln; PRMT5; Protein-Arginine N-Methyltransferases - genetics; Protein-Arginine N-Methyltransferases - metabolism; Proteins; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; Ribonucleoproteins, Small Nuclear - genetics; Ribonucleoproteins, Small Nuclear - metabolism; RNA, Small Nuclear - metabolism; SMN; SMN Complex Proteins - genetics; SMN Complex Proteins - metabolism; snRNP; Thermal energy; pICln; assembly; PRMT5; SMN; snRNP

The assembly of spliceosomal U snRNPs depends on the coordinated action of PRMT5 and SMN complexes in vivo . These trans ‐acting factors enable the faithful delivery of seven Sm proteins onto snRNA and the formation of the common core of snRNPs. To gain mechanistic insight into their mode of action,...