Functional mammalian spliceosomal complex E contains SMN complex proteins in addition to U1 and U2 snRNPs [PDF]
Spliceosomes remove introns from primary gene transcripts. They assemble de novo on each intron through a series of steps that involve the incorporation of five snRNP particles and multiple non-snRNP proteins. In mammals, all the intermediate complexes have been characterized on one transcript (MINX), with the exception of the very first, complex E. We
Makarov, E. M. +3 more
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Binding of the heterogeneous ribonucleoprotein K (hnRNP K) to the Epstein-Barr virus nuclear antigen 2 (EBNA2) enhances viral LMP2A expression. [PDF]
The Epstein-Barr Virus (EBV) -encoded EBNA2 protein, which is essential for the in vitro transformation of B-lymphocytes, interferes with cellular processes by binding to proteins via conserved sequence motifs.
Henrik Gross +16 more
doaj +3 more sources
NUFIP and the HSP90/R2TP chaperone bind the SMN complex and facilitate assembly of U4-specific proteins [PDF]
The Sm proteins are loaded on snRNAs by the SMN complex, but how snRNP-specific proteins are assembled remains poorly characterized. U4 snRNP and box C/D snoRNPs have structural similarities. They both contain the 15.5K and proteins with NOP domains (PRP31 for U4, NOP56/58 for snoRNPs).
Bizarro, Jonathan +8 more
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The survival of motor neurons (SMN) complex mediates the assembly of small nuclear ribonucleoproteins (snRNPs) involved in splicing and histone RNA processing. A crucial step in this process is the binding of Sm proteins onto the SMN protein. For Sm B/B', D1, and D3, efficient binding to SMN depends on symmetrical dimethyl arginine (sDMA) modifications
Azzouz, T. +7 more
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SECIS-binding protein 2 interacts with the SMN complex and the methylosome for selenoprotein mRNP assembly and translation [PDF]
Selenoprotein synthesis requires the co-translational recoding of a UGASec codon. This process involves an RNA structural element, called Selenocysteine Insertion Sequence (SECIS) and the SECIS binding protein 2 (SBP2). Several selenoprotein mRNAs undergo unusual cap hypermethylation by the trimethylguanosine synthase 1 (Tgs1), which is recruited by ...
Gribling-Burrer, Anne-Sophie +10 more
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SMN and coilin negatively regulate dyskerin association with telomerase RNA
Telomerase is a ribonucleoprotein comprising telomerase RNA and associated proteins. The formation of the telomerase holoenzyme takes place in the Cajal body (CB), a subnuclear domain that participates in the formation of ribonucleoproteins.
Aaron R. Poole, Michael D. Hebert
doaj +2 more sources
Composition of the Survival Motor Neuron (SMN) Complex in Drosophila melanogaster [PDF]
Spinal Muscular Atrophy (SMA) is caused by homozygous mutations in the human survival motor neuron 1 (SMN1) gene. SMN protein has a well-characterized role in the biogenesis of small nuclear ribonucleoproteins (snRNPs), core components of the spliceosome.
A. Gregory Matera +9 more
doaj +2 more sources
Pharmacological Activation of NRF2 by Omaveloxolone Upregulates NRF2-Target Proteins in SMA Type I Human Fibroblasts. [PDF]
SMA type I patient‐derived fibroblasts exhibit reduced basal NRF2 pathway output, reflected by decreased NQO1, xCT, and PGC1α. Pharmacological NRF2 activation with omaveloxolone (OMAV) increases cell viability and induces NRF2 target proteins in both control and SMA fibroblasts.
Vrettou S, Zetzsche S, Wirth B.
europepmc +2 more sources
WRAP53 is essential for Cajal body formation and for targeting the survival of motor neuron complex to Cajal bodies. [PDF]
The WRAP53 gene gives rise to a p53 antisense transcript that regulates p53. This gene also encodes a protein that directs small Cajal body-specific RNAs to Cajal bodies.
Salah Mahmoudi +7 more
doaj +1 more source
Association of galectin-1 and galectin-3 with Gemin4 in complexes containing the SMN protein [PDF]
In previous studies we showed that galectin-1 and galectin-3 are factors required for the splicing of pre-mRNA, as assayed in a cell-free system. Using a yeast two-hybrid screen with galectin-1 as bait, Gemin4 was identified as a putative interacting protein.
J W, Park +4 more
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