scholarly journals Staufen2 mediated RNA recognition and localization requires combinatorial action of multiple domains

2018 ◽  
Author(s):  
Simone Heber ◽  
Imre Gáspár ◽  
Jan-Niklas Tants ◽  
Johannes Günther ◽  
Sandra M. Fernandez Moya ◽  
...  
Keyword(s):  
Rna Binding ◽  
Mrna Localization ◽  
Rna Recognition ◽  
Double Stranded Rna ◽  
Binding Domains ◽  
Physiological Relevance ◽  
And Function ◽  
Necessary And Sufficient ◽  
Multiple Domains ◽  
Mrna Binding

AbstractThroughout metazoans, Staufen (Stau) proteins are core factors of mRNA localization particles. They consist of three to four double-stranded RNA binding domains (dsRBDs) and a C-terminal dsRBD-like domain. Mouse Staufen2 (mStau2) like Drosophila Stau (dmStau) contains four dsRBDs. Existing data suggest that only dsRBDs 3-4 are necessary and sufficient for mRNA binding. Here, we show that dsRBDs 1 and 2 of mStau2 bind RNA with similar affinities and kinetics as dsRBDs 3 and 4. While RNA binding by these tandem domains is transient, all four dsRBDs recognize their target RNAs with high stability. Rescue experiments in Drosophila oocytes demonstrate that mStau2 partially rescues dmStau-dependent mRNA localization. In contrast, a rescue with mStau2 bearing RNA-binding mutations in dsRBD1-2 fails, confirming the physiological relevance of our findings. In summary, our data show that the dsRBDs 1-2 play essential roles in the mRNA recognition and function of Stau- family proteins of different species.

scholarly journals Structural basis of si RNA recognition by TRBP double‐stranded RNA binding domains

2018 ◽  
Vol 37 (6) ◽  
Author(s):  
Gregoire Masliah ◽  
Christophe Maris ◽  
Sebastian LB König ◽  
Maxim Yulikov ◽  
Florian Aeschimann ◽  
...  
Keyword(s):  
Rna Binding ◽  
Structural Basis ◽  
Rna Recognition ◽  
Double Stranded Rna ◽  
Binding Domains ◽  
Rna Binding Domains ◽  
Si Rna

scholarly journals RNA Helicase A Regulates the Replication of RNA Viruses

Viruses ◽  
2021 ◽  
Vol 13 (3) ◽  
pp. 361
Author(s):  
Rui-Zhu Shi ◽  
Yuan-Qing Pan ◽  
Li Xing
Keyword(s):  
Virus Replication ◽  
Rna Binding ◽  
Rna Viruses ◽  
Rna Helicase ◽  
Rna Helicase A ◽  
Double Stranded Rna ◽  
Binding Domains ◽  
N Terminus

The RNA helicase A (RHA) is a member of DExH-box helicases and characterized by two double-stranded RNA binding domains at the N-terminus. RHA unwinds double-stranded RNA in vitro and is involved in RNA metabolisms in the cell. RHA is also hijacked by a variety of RNA viruses to facilitate virus replication. Herein, this review will provide an overview of the role of RHA in the replication of RNA viruses.

scholarly journals Double-stranded RNA drives SARS-CoV-2 nucleocapsid protein to undergo phase separation at specific temperatures

2021 ◽  
Author(s):  
Christine Roden ◽  
Yifan Dai ◽  
Ian Seim ◽  
Myungwoon Lee ◽  
Rachel Sealfon ◽  
...  
Keyword(s):  
Phase Separation ◽  
Rna Structure ◽  
Nucleocapsid Protein ◽  
Rna Binding ◽  
Genome Packaging ◽  
Rna Motifs ◽  
Double Stranded Rna ◽  
N Protein ◽  
Binding Domains

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.

Abstract P351: The Post-transcriptional Regulations Of Centrosomal Plp Mrna In Drosophila

2021 ◽  
Vol 129 (Suppl_1) ◽  
Author(s):  
Junnan Fang
Keyword(s):  
Translational Control ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Cell Types ◽  
Mrna Localization ◽  
Rna Localization ◽  
Embryonic Lethality ◽  
Cellular Processes ◽  
Pericentriolar Material ◽  
And Function

Centrosomes, functioning as microtubule organizing centers, are composed of a proteinaceous matrix of pericentriolar material (PCM) that surrounds a pair of centrioles. Drosophila Pericentrin (Pcnt)-like protein (PLP) is a key component of the centrosome that serves as a scaffold for PCM assembly. The disruption of plp in Drosophila results in embryonic lethality, while the deregulation of Pcnt in humans is associated with MOPD II and Trisomy 21.We recently found plp mRNA localizes to Drosophila embryonic centrosomes. While RNA is known to associate with centrosomes in diverse cell types, the elements required for plp mRNA localization to centrosomes remains completely unknown. Additionally, how plp translation is regulated to accommodate rapid cell divisions during early embryogenesis is unclear. RNA localization coupled with translational control is a conserved mechanism that functions in diverse cellular processes. Control of mRNA localization and translation is mediated by RNA-binding proteins (RBPs). We find PLP protein expression is specifically promoted by an RNA-binding protein, Orb, during embryogenesis; moreover, plp mRNA interacts with Orb. Importantly, we find overexpression of full-length PLP can rescue cell division defects and embryonic lethality caused by orb depletion. We aim to uncover the mechanisms underlying embryonic plp mRNA localization and function and how Orb regulates plp translation.

scholarly journals RNA-Regulated Interaction of Transportin-1 and Exportin-5 with the Double-Stranded RNA-Binding Domain Regulates Nucleocytoplasmic Shuttling of ADAR1

2009 ◽  
Vol 29 (6) ◽  
pp. 1487-1497 ◽  
Author(s):  
Jutta Fritz ◽  
Alexander Strehblow ◽  
Andreas Taschner ◽  
Sandy Schopoff ◽  
Pawel Pasierbek ◽  
...  
Keyword(s):  
Nuclear Export ◽  
Rna Binding ◽  
Nuclear Export Signal ◽  
Nucleocytoplasmic Transport ◽  
Nucleocytoplasmic Shuttling ◽  
Double Stranded Rna ◽  
Binding Domains ◽  
Dsrna Binding ◽  
Localization Signal ◽  
Editing Enzyme

ABSTRACT Double-stranded RNA (dsRNA)-binding proteins interact with substrate RNAs via dsRNA-binding domains (dsRBDs). Several proteins harboring these domains exhibit nucleocytoplasmic shuttling and possibly remain associated with their substrate RNAs bound in the nucleus during nuclear export. In the human RNA-editing enzyme ADAR1-c, the nuclear localization signal overlaps the third dsRBD, while the corresponding import factor is unknown. The protein also lacks a clear nuclear export signal but shuttles between the nucleus and the cytoplasm. Here we identify transportin-1 as the import receptor for ADAR1. Interestingly, dsRNA binding interferes with transportin-1 binding. At the same time, each of the dsRBDs in ADAR1 interacts with the export factor exportin-5. RNA binding stimulates this interaction but is not a prerequisite. Thus, our data demonstrate a role for some dsRBDs as RNA-sensitive nucleocytoplasmic transport signals. dsRBD3 in ADAR1 can mediate nuclear import, while interaction of all dsRBDs might control nuclear export. This finding may have implications for other proteins containing dsRBDs and suggests a selective nuclear export mechanism for substrates interacting with these proteins.

scholarly journals Recognition of viral RNA stem-loops by the tandem double-stranded RNA binding domains of PKR

RNA ◽  
2013 ◽  
Vol 19 (3) ◽  
pp. 333-344 ◽  
Author(s):  
E. Dzananovic ◽  
T. R. Patel ◽  
S. Deo ◽  
K. McEleney ◽  
J. Stetefeld ◽  
...  
Keyword(s):  
Rna Binding ◽  
Viral Rna ◽  
Double Stranded Rna ◽  
Binding Domains ◽  
Rna Binding Domains

scholarly journals The N-Terminal Double-Stranded RNA Binding Domains of Arabidopsis HYPONASTIC LEAVES1 Are Sufficient for Pre-MicroRNA Processing

2007 ◽  
Vol 19 (3) ◽  
pp. 914-925 ◽  
Author(s):  
Feijie Wu ◽  
Lin Yu ◽  
Wenguang Cao ◽  
Yanfei Mao ◽  
Zhongyuan Liu ◽  
...  
Keyword(s):  
Rna Binding ◽  
Double Stranded Rna ◽  
Binding Domains ◽  
Microrna Processing ◽  
Rna Binding Domains
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