scholarly journals Pseudo-RNA-Binding Domains Mediate RNA Structure Specificity in Upstream of N-Ras

Cell Reports ◽  
2020 ◽  
Vol 32 (3) ◽  
pp. 107930 ◽  
Author(s):  
Nele Merret Hollmann ◽  
Pravin Kumar Ankush Jagtap ◽  
Pawel Masiewicz ◽  
Tanit Guitart ◽  
Bernd Simon ◽  
...  
2020 ◽  
Author(s):  
Nele Merret Hollmann ◽  
Pravin Kumar Ankush Jagtap ◽  
Pawel Masiewicz ◽  
Tanit Guitart ◽  
Bernd Simon ◽  
...  

Genetics ◽  
2001 ◽  
Vol 159 (4) ◽  
pp. 1617-1630
Author(s):  
Suk-Won Jin ◽  
Nancy Arno ◽  
Adam Cohen ◽  
Amy Shah ◽  
Qijin Xu ◽  
...  

Abstract FOG-1 controls germ cell fates in the nematode Caenorhabditis elegans. Sequence analyses revealed that FOG-1 is a cytoplasmic polyadenylation element binding (CPEB) protein; similar proteins from other species have been shown to bind messenger RNAs and regulate their translation. Our analyses of fog-1 mutations indicate that each of the three RNA-binding domains of FOG-1 is essential for activity. In addition, biochemical tests show that FOG-1 is capable of binding RNA sequences in the 3′-untranslated region of its own message. Finally, genetic assays reveal that fog-1 functions zygotically, that the small fog-1 transcript has no detectable function, and that missense mutations in fog-1 cause a dominant negative phenotype. This last observation suggests that FOG-1 acts in a complex, or as a multimer, to regulate translation. On the basis of these data, we propose that FOG-1 binds RNA to regulate germ cell fates and that it does so by controlling the translation of its targets. One of these targets might be the fog-1 transcript itself.


2004 ◽  
Vol 337 (4) ◽  
pp. 799-816 ◽  
Author(s):  
Carina Johansson ◽  
L.David Finger ◽  
Lukas Trantirek ◽  
Thomas D Mueller ◽  
Soyoun Kim ◽  
...  

2021 ◽  
Author(s):  
Christine Roden ◽  
Yifan Dai ◽  
Ian Seim ◽  
Myungwoon Lee ◽  
Rachel Sealfon ◽  
...  

Betacoronavirus SARS-CoV-2 infections caused the global Covid-19 pandemic. The nucleocapsid protein (N-protein) is required for multiple steps in the betacoronavirus replication cycle. SARS-CoV-2-N-protein is known to undergo liquid-liquid phase separation (LLPS) with specific RNAs at particular temperatures to form condensates. We show that N-protein recognizes at least two separate and distinct RNA motifs, both of which require double-stranded RNA (dsRNA) for LLPS. These motifs are separately recognized by N-protein's two RNA binding domains (RBDs). Addition of dsRNA accelerates and modifies N-protein LLPS in vitro and in cells and controls the temperature condensates form. The abundance of dsRNA tunes N-protein-mediated translational repression and may confer a switch from translation to genome packaging. Thus, N-protein's two RBDs interact with separate dsRNA motifs, and these interactions impart distinct droplet properties that can support multiple viral functions. These experiments demonstrate a paradigm of how RNA structure can control the properties of biomolecular condensates.


1997 ◽  
Vol 272 (20) ◽  
pp. 13109-13116 ◽  
Author(s):  
Guillaume Serin ◽  
Gérard Joseph ◽  
Laurence Ghisolfi ◽  
Marielle Bauzan ◽  
Monique Erard ◽  
...  

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