TY  - JOUR
A1  - Ji, Changhe
A1  - Bader, Jakob
A1  - Ramanathan, Pradhipa
A1  - Hennlein, Luisa
A1  - Meissner, Felix
A1  - Jablonka, Sibylle
A1  - Mann, Matthias
A1  - Fischer, Utz
A1  - Sendtner, Michael
A1  - Briese, Michael
T1  - Interaction of 7SK with the Smn complex modulates snRNP production
JF  - Nature Communications
N2  - Gene expression requires tight coordination of the molecular machineries that mediate transcription and splicing. While the interplay between transcription kinetics and spliceosome fidelity has been investigated before, less is known about mechanisms regulating the assembly of the spliceosomal machinery in response to transcription changes. Here, we report an association of the Smn complex, which mediates spliceosomal snRNP biogenesis, with the 7SK complex involved in transcriptional regulation. We found that Smn interacts with the 7SK core components Larp7 and Mepce and specifically associates with 7SK subcomplexes containing hnRNP R. The association between Smn and 7SK complexes is enhanced upon transcriptional inhibition leading to reduced production of snRNPs. Taken together, our findings reveal a functional association of Smn and 7SK complexes that is governed by global changes in transcription. Thus, in addition to its canonical nuclear role in transcriptional regulation, 7SK has cytosolic functions in fine-tuning spliceosome production according to transcriptional demand.
KW  - Molecular neuroscience
KW  - RNA
KW  - RNA splicing
KW  - Transcription
Y1  - 2021
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-259125
VL  - 12
IS  - 1
ER  - 
TY  - JOUR
A1  - Veepaschit, Jyotishman
A1  - Viswanathan, Aravindan
A1  - Bordonne, Remy
A1  - Grimm, Clemens
A1  - Fischer, Utz
T1  - Identification and structural analysis of the Schizosaccharomyces pombe SMN complex
JF  - Nucleic Acids Research
N2  - The macromolecular SMN complex facilitates the formation of Sm-class ribonucleoproteins involved in mRNA processing (UsnRNPs). While biochemical studies have revealed key activities of the SMN complex, its structural investigation is lagging behind. Here we report on the identification and structural determination of the SMN complex from the lower eukaryote Schizosaccharomyces pombe, consisting of SMN, Gemin2, 6, 7, 8 and Sm proteins. The core of the SMN complex is formed by several copies of SMN tethered through its C-terminal alpha-helices arranged with alternating polarity. This creates a central platform onto which Gemin8 binds and recruits Gemins 6 and 7. The N-terminal parts of the SMN molecules extrude via flexible linkers from the core and enable binding of Gemin2 and Sm proteins. Our data identify the SMN complex as a multivalent hub where Sm proteins are collected in its periphery to allow their joining with UsnRNA.
KW  - Schizosaccharomyces pombe
KW  - SMN
Y1  - 2021
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-259880
VL  - 49
IS  - 13
ER  -