Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43

2013 ◽  
Vol 20 (12) ◽  
pp. 1443-1449 ◽  
Author(s):  
Peter J Lukavsky ◽  
Dalia Daujotyte ◽  
James R Tollervey ◽  
Jernej Ule ◽  
Cristiana Stuani ◽  
...  
Keyword(s):  
Molecular Basis ◽  
Splicing Factor ◽  
Rna Recognition

scholarly journals Molecular basis of RNA recognition by the human alternative splicing factor Fox-1

2005 ◽  
Vol 25 (1) ◽  
pp. 163-173 ◽  
Author(s):  
Sigrid D Auweter ◽  
Rudi Fasan ◽  
Luc Reymond ◽  
Jason G Underwood ◽  
Douglas L Black ◽  
...  
Keyword(s):  
Alternative Splicing ◽  
Molecular Basis ◽  
Splicing Factor ◽  
Rna Recognition ◽  
Alternative Splicing Factor

scholarly journals Characterization of the Molecular Basis of Group II Intron RNA Recognition by CRS1-CRM Domains

2008 ◽  
Vol 283 (34) ◽  
pp. 23333-23342 ◽  
Author(s):  
Ido Keren ◽  
Liron Klipcan ◽  
Ayenachew Bezawork-Geleta ◽  
Max Kolton ◽  
Felix Shaya ◽  
...  
Keyword(s):  
Molecular Basis ◽  
Group Ii Intron ◽  
Rna Recognition ◽  
Group Ii

scholarly journals The molecular basis for ANE syndrome revealed by the large ribosomal subunit processome interactome

eLife ◽  
2016 ◽  
Vol 5 ◽  
Author(s):  
Kathleen L McCann ◽  
Takamasa Teramoto ◽  
Jun Zhang ◽  
Traci M Tanaka Hall ◽  
Susan J Baserga
Keyword(s):  
Protein Interactions ◽  
Molecular Basis ◽  
Large Subunit ◽  
Ribosomal Subunit ◽  
Rna Recognition Motif ◽  
Rna Recognition ◽  
Rrna Processing ◽  
Protein Protein Interactions ◽  
Recognition Motif ◽  
Processing Defects

ANE syndrome is a ribosomopathy caused by a mutation in an RNA recognition motif of RBM28, a nucleolar protein conserved to yeast (Nop4). While patients with ANE syndrome have fewer mature ribosomes, it is unclear how this mutation disrupts ribosome assembly. Here we use yeast as a model system and show that the mutation confers growth and pre-rRNA processing defects. Recently, we found that Nop4 is a hub protein in the nucleolar large subunit (LSU) processome interactome. Here we demonstrate that the ANE syndrome mutation disrupts Nop4’s hub function by abrogating several of Nop4’s protein-protein interactions. Circular dichroism and NMR demonstrate that the ANE syndrome mutation in RRM3 of human RBM28 disrupts domain folding. We conclude that the ANE syndrome mutation generates defective protein folding which abrogates protein-protein interactions and causes faulty pre-LSU rRNA processing, thus revealing one aspect of the molecular basis of this human disease.

Structural and dynamic studies of the human RNA binding protein RBM3 reveals the molecular basis of its oligomerization and RNA recognition

FEBS Journal ◽  
2021 ◽  
Author(s):  
Sayantani Roy ◽  
Soumendu Boral ◽  
Snigdha Maiti ◽  
Tushar Kushwaha ◽  
Aditya J. Basak ◽  
...  
Keyword(s):  
Molecular Basis ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Rna Recognition ◽  
Dynamic Studies

scholarly journals Molecular Basis for Target RNA Recognition and Cleavage by Human RISC

Cell ◽  
2007 ◽  
Vol 130 (1) ◽  
pp. 101-112 ◽  
Author(s):  
Stefan Ludwig Ameres ◽  
Javier Martinez ◽  
Renée Schroeder
Keyword(s):  
Molecular Basis ◽  
Rna Recognition ◽  
Target Rna

scholarly journals Structure and Interactions of the First Three RNA Recognition Motifs of Splicing Factor Prp24

2007 ◽  
Vol 367 (5) ◽  
pp. 1447-1458 ◽  
Author(s):  
Euiyoung Bae ◽  
Nicholas J. Reiter ◽  
Craig A. Bingman ◽  
Sharon S. Kwan ◽  
Donghan Lee ◽  
...  
Keyword(s):  
Splicing Factor ◽  
Rna Recognition ◽  
Rna Recognition Motifs ◽  
Recognition Motifs

scholarly journals Directional Phosphorylation and Nuclear Transport of the Splicing Factor SRSF1 Is Regulated by an RNA Recognition Motif

2016 ◽  
Vol 428 (11) ◽  
pp. 2430-2445 ◽  
Author(s):  
Pedro Serrano ◽  
Brandon E. Aubol ◽  
Malik M. Keshwani ◽  
Stefano Forli ◽  
Chen-Ting Ma ◽  
...  
Keyword(s):  
Nuclear Transport ◽  
Splicing Factor ◽  
Rna Recognition Motif ◽  
Rna Recognition ◽  
Recognition Motif

scholarly journals Rice Floury Shrunken Endosperm5 encodes a putative plant organelle RNA recognition protein that is required for cis-splicing of mitochondrial nad4 intron 1

2020 ◽  
Author(s):  
Liang Wang ◽  
Wenwei Zhang ◽  
Shijia Liu ◽  
Yunlu Tian ◽  
Xi Liu ◽  
...  
Keyword(s):  
Complex I ◽  
Nadh Dehydrogenase ◽  
Higher Plants ◽  
Splicing Factor ◽  
Rna Recognition ◽  
Loss Of Function ◽  
Rice Mutant ◽  
Intron 1 ◽  
Recognition Protein ◽  
Underlying Mechanisms

Abstract Background: Some important mitochondrial-encoded genes for respiration in higher plants are interrupted by introns. Many nuclear-encoded factors are involved in the splicing of these introns, but the underlying mechanisms remain to be deciphered.Results: Here, we isolated and characterized a rice mutant named floury shrunken endosperm5 (fse5). In addition to floury shrunken endosperm seeds with mutant phenotype either failed to germinate or produced retarded lethal seedlings. The Fse5 encodes a putative plant organelle RNA recognition (PORR) protein targeted to mitochondria. Mutation of Fse5 hindered splicing of the first intron of nad4, that encodes an essential subunit of mitochondrial NADH dehydrogenase Complex I. The assembly and NADH dehydrogenase activity of Complex I were disrupted and the structure of the mitochondria was abnormal in the fse5 mutant. FSE5 protein was shown to interact with Mitochondrial Intron Splicing Factor 68 (MISF68), which is also a splicing factor for nad4 intron 1 identified previously in a yeast two-hybrid assay.Conclusion: Fse5 encoding a PORR protein is essential for splicing of nad4 intron 1, and loss of function affects seed development and seedling growth.

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