Ilf3 and NF90 associate with the axonal targeting element of Tau mRNA

Larcher, Jean-Christophe; Gasmi, Laïla; Viranaïcken, Wildriss; Eddé, Bernard; Bernard, Rozenn; Ginzburg, Irith; Denoulet, Philippe

doi:10.1096/fj.04-1763fje

Cited by 48 publications

(48 citation statements)

References 44 publications

(69 reference statements)

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“…Besides the partner proteins for the Dicer and Drosha families, at least one other protein family, the NFAT family, also encodes tandem DSRMs. The NFAT family proteins, which contain a DZF protein domain in addition to tandem DSRMs, are putative nuclear, nucleotide transferases that participate in DNA repair and RNA transport (32,59,60,73; reviewed in reference 31). Further study of DRB1 and DRB2 in T. thermophila may reveal new roles for tandem DSRM-containing proteins.…”

Section: Discussionmentioning

confidence: 99%

Zygotic Expression of the Double-Stranded RNA Binding Motif Protein Drb2p Is Required for DNA Elimination in the Ciliate Tetrahymena thermophila

Motl

Chalker

2011

Eukaryot Cell

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Double-stranded RNA binding motif (DSRM)-containing proteins play many roles in the regulation of gene transcription and translation, including some with tandem DSRMs that act in small RNA biogenesis. We report the characterization of the genes for double-stranded RNA binding proteins 1 and 2 (DRB1 and DRB2), two genes encoding nuclear proteins with tandem DSRMs in the ciliate Tetrahymena thermophila. Both proteins are expressed throughout growth and development but exhibit distinct peaks of expression, suggesting different biological roles. In support of this, we show that expression of DRB2 is essential for vegetative growth while DRB1 expression is not. During conjugation, Drb1p and Drb2p localize to distinct nuclear foci. Cells lacking all DRB1 copies are able to produce viable progeny, although at a reduced rate relative to wild-type cells. In contrast, cells lacking germ line DRB2 copies, which thus cannot express Drb2p zygotically, fail to produce progeny, arresting late into conjugation. This arrest phenotype is accompanied by a failure to organize the essential DNA rearrangement protein Pdd1p into DNA elimination bodies and execute DNA elimination and chromosome breakage. These results implicate zygotically expressed Drb2p in the maturation of these nuclear structures, which are necessary for reorganization of the somatic genome.Proteins containing a double-stranded RNA (dsRNA) binding motif (DSRM) participate in diverse biological pathways in a wide range of organisms. This motif was first identified in the developmentally essential gene Staufen of Drosophila melanogaster and has since been recognized to be encoded in the genomes in all three domains of living organisms, as well as in viruses (63; reviewed in references 20 and 67). DSRM proteins commonly act in developmental pathways (e.g., RNA localization by the Staufen family and developmental transcriptional regulation by the DIP1 family) (5,18,62,68) but also have ubiquitous roles in transcriptional and translational regulation (e.g., PKR family and PKR-associated proteins) (26,45,55,58). Proteins vital for RNA interference (RNAi) also contain DSRMs. These include members of the RNase III family (e.g., Dicer and Drosha family proteins) and their tandem DSRMcontaining partner proteins (e.g., RDE-4 of Caenorhabditis elegans, Pasha, R2D2, and Loqs in D. melanogaster, and their homologues in

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Section: Discussionmentioning

confidence: 99%

Zygotic Expression of the Double-Stranded RNA Binding Motif Protein Drb2p Is Required for DNA Elimination in the Ciliate Tetrahymena thermophila

Motl

Chalker

2011

Eukaryot Cell

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“…The cells were lysed by sonication on ice and centrifuged for 5 min at 16,000 ϫ g, and the supernatant was retained as cell extract. Mouse brain extracts were obtained as previously described (24). The protein concentrations of extracts were determined using the Micro BCA Protein Assay Reagent Kit (Pierce), with bovine serum albumin used as a standard.…”

Section: Methodsmentioning

confidence: 99%

Involvement of Human Release Factors eRF3a and eRF3b in Translation Termination and Regulation of the Termination Complex Formation

Chauvin

Salhi

Goff

et al. 2005

Molecular and Cellular Biology

107

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eRF3 is a GTPase associated with eRF1 in a complex that mediates translation termination in eukaryotes. In mammals, two genes encode two distinct forms of eRF3, eRF3a and eRF3b, which differ in their N-terminal domains. Both bind eRF1 and stimulate its release activity in vitro. However, whether both proteins can function as termination factors in vivo has not been determined. In this study, we used short interfering RNAs to examine the effect of eRF3a and eRF3b depletion on translation termination efficiency in human cells. By measuring the readthrough at a premature nonsense codon in a reporter mRNA, we found that eRF3a silencing induced an important increase in readthrough whereas eRF3b silencing had no significant effect. We also found that eRF3a depletion reduced the intracellular level of eRF1 protein by affecting its stability. In addition, we showed that eRF3b overexpression alleviated the effect of eRF3a silencing on readthrough and on eRF1 cellular levels. These results suggest that eRF3a is the major factor acting in translation termination in mammals and clearly demonstrate that eRF3b can substitute for eRF3a in this function. Finally, our data indicate that the expression level of eRF3a controls the formation of the termination complex by modulating eRF1 protein stability.In eukaryotes, two release factors, eRF1 and eRF3, are required to complete protein synthesis. These translation termination factors associate in a complex which binds to the elongating ribosome when a stop codon enters the A site. eRF1 recognizes all three stop codons by direct interaction at the decoding A site (5, 10) and activates the peptidyltransferase center, which triggers the hydrolysis of the peptidyltRNA, generating a free full-sized polypeptide. eRF3 is a GTPase that stimulates eRF1 activity in a GTP-dependent manner (40). eRF3 alone can bind GTP, but its GTPase activity requires the presence of both eRF1 and ribosomes, which may play the role of a composite GTPase-activating protein (11, 12). The eRF3 GTP-bound form interacts with eRF1 in vitro and in vivo to constitute the active translation termination complex (12,36,40). In the yeast Saccharomyces cerevisiae, eRF1 and eRF3 are encoded by the essential genes SUP45 and SUP35, respectively. Mutations in either of these genes cause an omnipotent suppressor phenotype and the ability to enhance nonsense suppression by a weak suppressor tRNA (reviewed in reference 18). Recently, it has been shown in S. cerevisiae that eRF3 GTPase activity facilitates stop codon decoding by eRF1 (33).The C-terminal regions of eRF3 proteins are highly conserved through evolution and carry the four canonical GTPbinding motifs of the GTPase superfamily (2). This domain is essential for translation termination and interaction with eRF1. The N-terminal region varies in both length and sequence among species. In yeast, it is neither essential for cell viability nor required for termination but is responsible for prion-like [PSI ϩ ] factor formation (29, 31). Otherwise, this domain participates in...

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“…Besides transcription regulation, NFAR1 and NFAR2 bind to AU-rich elements in the 3Ј-untranslated region of mRNAs and regulate their stabilization, localization, and translation. For example, NFAR1/2 bind to and stabilize interleukin-2 and mitogen-activated protein kinase phosphatase-1 mRNAs (29,30) and bind to the 3Ј-untranslated region of Tau mRNA, which is known as an element required for its transport to the axon in neurons (31). NFAR1/2 also inhibit global translation as well as bind to viral RNA and prevent its translation (32,33).…”

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confidence: 99%

RNA Granule Assembly and Disassembly Modulated by Nuclear Factor Associated with Double-stranded RNA 2 and Nuclear Factor 45

Shiina

Nakayama

2014

Journal of Biological Chemistry

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Background: RNA granules are associated with translational control and neurodegenerative disease. Results: Nuclear factor associated with dsRNA 2 (NFAR2) enhances RNA granule assembly through two domains, one of which is antagonized by nuclear factor 45 (NF45). Conclusion: NFAR2 and NF45 play novel regulatory roles in RNA granule assembly and disassembly. Significance: Mechanisms of RNA granule assembly and disassembly are the basis for understanding translational control and neurodegenerative disease.

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Ilf3 and NF90 associate with the axonal targeting element of Tau mRNA

Cited by 48 publications

References 44 publications

Zygotic Expression of the Double-Stranded RNA Binding Motif Protein Drb2p Is Required for DNA Elimination in the Ciliate Tetrahymena thermophila

Zygotic Expression of the Double-Stranded RNA Binding Motif Protein Drb2p Is Required for DNA Elimination in the Ciliate Tetrahymena thermophila

Involvement of Human Release Factors eRF3a and eRF3b in Translation Termination and Regulation of the Termination Complex Formation

RNA Granule Assembly and Disassembly Modulated by Nuclear Factor Associated with Double-stranded RNA 2 and Nuclear Factor 45

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