Komal Soni
@Komal_Soni02
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Staff Scientist @UniBayreuth Passionate about structural biology of protein-RNA complexes
Joined October 2021
Spliceosomes use quality control mechanisms to detect and correct mistakes during RNA processing. Our work explores how defective spliceosomes are identified and discarded. #RNA #RNAProcessing #Spliceosomes #QualityControlMechanisms #RMAP.
nature.com
Nature Structural & Molecular Biology - Here, the authors provide insights into a splicing quality control mechanism. The Gpl1–Gih35 complex binds to the active site of aberrant...
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RT @Mel_McDowell22: Proud to share our first lab pre-print: “SND3 is the membrane insertase within a fungal multipass translocon” where @Tz….
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RT @GlattSebastian: We are very excited about our latest work, which just came out @embojournal – The work @MCB_UJ….
embopress.org
imageimagetRNAs harbour a complex set of modifications which are important for their function. Here, single particle cryo-EM, biophysics, and computational analyses of the effects of pseudouridine...
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RT @naturemethods: Introducing spIsoNet, a software tool that addresses the challenges of map anisotropy and particle misalignment in cryo-….
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We propose that the Gpl1-Gih35 complex is involved in a new Splicing Quality Control mechanism in the discard pathway where it initiates the process of disassembly by the Ntr1 complex. (7/7)
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Structure superpositions with Bact and B* spliceosomes suggest that Gih35 likely acts on the branch helix in the process of disassembly. (6/7)
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Gpl1 has an enormous interface with Prp8 and acts as a molecular glue between Gih35 and the spliceosome. (5/7)
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Gpl1 recognizes this altered active site conformation. The largely unstructured Gpl1 crawls into the active site where it also extensively interacts with the 1585-loop of Prp8. (4/7)
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We find an insertion at the active site of the Bd complex, which changes the conformation of the pre-mRNA causing an aberration. RNA-seq data confirm our structural observations. (3/7)
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We have isolated post-Bact aberrant spliceosomes assembled on unspliced pre-mRNA substrates, primed for discard (Bd). (2/7)
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📢Delighted to share our preprint on cryo-EM structures of aberrant spliceosome intermediates from Schizosaccharomyces pombe. This work sheds light on a new splicing quality control mechanism. Check out the full paper here: (1/7).
biorxiv.org
Intron removal during pre-mRNA splicing is of extraordinary complexity and its disruption causes a vast number of genetic diseases in humans[1][1]. While key steps of the canonical spliceosome cycle...
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Gpl1 has an enormous interface with Prp8 and acts as a molecular glue between Gih35 and the spliceosome. (5/7)
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Gpl1 recognizes this altered active site conformation. The largely unstructured Gpl1 crawls into the active site where it also extensively interacts with the 1585-loop of Prp8. (4/7)
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We find an insertion at the active site of the Bd complex, which changes the conformation of the pre-mRNA causing an aberration. RNA-seq data confirm our structural observations. (3/7)
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We have isolated post-Bact aberrant spliceosomes assembled on unspliced pre-mRNA substrates, primed for discard (Bd).
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RT @MolecularCell: eIF4F is a thermo-sensing regulatory node in the translational heat shock response
cell.com
Using reconstitution biochemistry and experiments in yeast cells, Desroches Altamirano et al. demonstrate that a heat-induced conformational rearrangement in eIF4G dissociates eIF4A from eIF4F and...
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RT @AbdelWahablab: Excited to announce our paper out today in @MolecularCell discovering a novel splicing factor GPATCH8 and its requiremen….
cell.com
Mutations in the RNA splicing factor SF3B1 are common in cancer and result in widespread alterations in splicing. Here, Benbarche et al. identify GPATCH8 as a novel splicing factor required for...
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RT @Jeske_Lab: Struggling with testing interactions between structurally complex proteins? -> You may try ReLo. Great work by x-less Harp….
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RT @embl: The Hennig group provided insights into the basic unwinding reaction of a key RNA helicase in the fruit fly. The study illustrat….
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