scholarly journals RBD-1, a nucleolar RNA-binding protein, is essential for Caenorhabditis elegans early development through 18S ribosomal RNA processing

2004 ◽  
Vol 32 (3) ◽  
pp. 1028-1036 ◽  
Author(s):  
E. Saijou
Keyword(s):  
Caenorhabditis Elegans ◽  
Early Development ◽  
Ribosomal Rna ◽  
Rna Processing ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
18S Ribosomal Rna ◽  
Ribosomal Rna Processing ◽  
Nucleolar Rna

scholarly journals Human cytomegalovirus induces and exploits Roquin to counteract the IRF1-mediated antiviral state

2019 ◽  
Vol 116 (37) ◽  
pp. 18619-18628 ◽  
Author(s):  
Jaewon Song ◽  
Sanghyun Lee ◽  
Dong-Yeon Cho ◽  
Sungwon Lee ◽  
Hyewon Kim ◽  
...  
Keyword(s):  
Human Cytomegalovirus ◽  
Rna Processing ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Transcriptome Profiling ◽  
Loss Of Function ◽  
Antiviral Genes ◽  
Cellular Antiviral Response ◽  
Infected Cells

RNA represents a pivotal component of host–pathogen interactions. Human cytomegalovirus (HCMV) infection causes extensive alteration in host RNA metabolism, but the functional relationship between the virus and cellular RNA processing remains largely unknown. Through loss-of-function screening, we show that HCMV requires multiple RNA-processing machineries for efficient viral lytic production. In particular, the cellular RNA-binding protein Roquin, whose expression is actively stimulated by HCMV, plays an essential role in inhibiting the innate immune response. Transcriptome profiling revealed Roquin-dependent global down-regulation of proinflammatory cytokines and antiviral genes in HCMV-infected cells. Furthermore, using cross-linking immunoprecipitation (CLIP)-sequencing (seq), we identified IFN regulatory factor 1 (IRF1), a master transcriptional activator of immune responses, as a Roquin target gene. Roquin reduces IRF1 expression by directly binding to its mRNA, thereby enabling suppression of a variety of antiviral genes. This study demonstrates how HCMV exploits host RNA-binding protein to prevent a cellular antiviral response and offers mechanistic insight into the potential development of CMV therapeutics.

scholarly journals Transcriptome-Wide Identification of RNA Targets of Arabidopsis SERINE/ARGININE-RICH45 Uncovers the Unexpected Roles of This RNA Binding Protein in RNA Processing

2015 ◽  
Vol 27 (12) ◽  
pp. 3294-3308 ◽  
Author(s):  
Denghui Xing ◽  
Yajun Wang ◽  
Michael Hamilton ◽  
Asa Ben-Hur ◽  
Anireddy S.N. Reddy
Keyword(s):  
Rna Processing ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Rna Targets

scholarly journals Multiple Mechanisms Inactivate the LIN-41 RNA-Binding Protein to Ensure A Robust Oocyte-to-Embryo Transition in Caenorhabditis elegans

2018 ◽  
Author(s):  
Caroline A. Spike ◽  
Gabriela Huelgas-Morales ◽  
Tatsuya Tsukamoto ◽  
David Greenstein
Keyword(s):  
Caenorhabditis Elegans ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Adaptor Protein ◽  
Protein Translation ◽  
Translational Repression ◽  
Meiotic Maturation ◽  
Oocyte Growth ◽  
Translational Repressor

ABSTRACTIn the nematode Caenorhabditis elegans, the conserved LIN-41 RNA-binding protein is a translational repressor that coordinately controls oocyte growth and meiotic maturation. LIN-41 exerts these effects, at least in part, by preventing the premature activation of the cyclin-dependent kinase CDK-1. Here we investigate the mechanism by which LIN-41 is rapidly eliminated upon the onset of meiotic maturation. Elimination of LIN-41 requires the activities of CDK-1 and multiple SCF-type ubiquitin ligase subunits, including the conserved substrate adaptor protein SEL-10/Fbw7/Cdc4, suggesting that LIN-41 is a target of ubiquitin-mediated protein degradation. Within the LIN-41 protein, two non-overlapping regions, Deg-A and Deg-B, are individually necessary for LIN-41 degradation; both contain several potential phosphodegron sequences, and at least one of these sites is required for LIN-41 degradation. Finally, Deg-A and Deg-B are sufficient, in combination, to mediate SEL-10-dependent degradation when transplanted into a different oocyte protein. Although LIN-41 is a potent inhibitor of protein translation and M-phase entry, the failure to eliminate LIN-41 from early embryos does not result in the continued translational repression of LIN-41 oocyte mRNA targets. Based on these observations, we propose a molecular model for the elimination of LIN-41 by SCFSEL-10 and suggest that LIN-41 is inactivated before it is degraded. Furthermore, we provide evidence that another RNA-binding protein, the GLD-1 tumor suppressor, is regulated similarly. Redundant mechanisms to extinguish translational repression by RNA-binding proteins may both control and provide robustness to irreversible developmental transitions, including meiotic maturation and the oocyte-to-embryo transition.

Abstract 204: Molecular function of the RNA binding protein EWS in RNA processing

2012 ◽  
Author(s):  
Bethsaida I. Nieves ◽  
Shuang Niu ◽  
Dedeepya Vaka ◽  
Julia Salzman ◽  
Patrick Brown ◽  
...  
Keyword(s):  
Rna Processing ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Molecular Function

Solution structure of the ribosomal RNA binding protein S15 from Thermus thermophilus

1997 ◽  
Vol 4 (1) ◽  
pp. 20-23 ◽  
Author(s):  
Helena Berglund ◽  
Alexey Rak ◽  
Alexander Serganov ◽  
Maria Garber ◽  
Torleif Härd
Keyword(s):  
Ribosomal Rna ◽  
Solution Structure ◽  
Rna Binding ◽  
Binding Protein ◽  
Thermus Thermophilus ◽  
Rna Binding Protein
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