Identification and functional characterization of a TIA-1-related nucleolysin.

Kawakami, Atsushi; Tian, Qingsheng; Duan, Xiaochu; Streuli, Michel; Schlossman, Stuart F.; Anderson, Patricia

doi:10.1073/pnas.89.18.8681

Cited by 155 publications

(129 citation statements)

References 27 publications

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“…Plant RBPs in the second clade showed strong homologies to T-cell-restricted intracellular antigen (TIA-1) and TIA-1-related protein (TIAR), both of which function as mRNA turnover and translation regulatory (TTR) RBPs (MazanMamczarz et al, 2006;Pullmann et al, 2007). TIA-1 and TIAR also are involved in signaling apoptotic cell death in mammalian systems (Kawakami et al, 1992;Taupin et al, 1995;Tian et al, 1991) and are important players in oxidative stress signaling (Abdelmohsen et al, 2008).…”

Section: Discussionmentioning

confidence: 99%

Phylogenetic and Expression Analysis of RNA-binding Proteins with Triple RNA Recognition Motifs in Plants

Peal¹,

Jambunathan²,

Mahalingam³

2011

Molecules and Cells

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The superfamily of RNA binding proteins (RBPs) is vastly expanded in plants compared to other eukaryotes. A subfamily of RBPs that contain three RNA recognition motifs (RRMs) from the Arabidopsis (24), rice (19) and poplar (37) genomes was analyzed in this study. Phylogenetic analysis with full-length protein sequences of 80 RBPs identified nine clades. The largest clade, comprising 23 members, showed high homology to human RBPs involved in oxidative signaling. Digital northern analysis revealed that Arabidopsis RBPs are transcriptionally responsive to biotic, abiotic and hormonal treatments. Northern blot analysis of eight Arabidopsis RBPs belonging to the tobacco RBP45/47 family showed that these genes respond to ozone stress. AtRBP45b, which shows closest homology to the yeast oxidative stress regulatory protein, CSX1, was expressed in multiple tissues. Two novel splice variant forms of AtRBP45b were identified by 3'RACE analysis. Based on RT-PCR, splice variant AtRBP45b-SV1 was observed only in response to mechanical wounding caused by pathogen or chemical infiltrations and was not detectable in response to salt or temperature stress. Electrophoretic mobility shift assay demonstrated that recombinant full-length and splice variant forms of AtRBP45b bound synthetic RNA. Identifying in vivo RNA targets of AtRBP45b will aid in determining the precise functional role of these proteins during oxidative signaling.

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Section: Discussionmentioning

confidence: 99%

Phylogenetic and Expression Analysis of RNA-binding Proteins with Triple RNA Recognition Motifs in Plants

Peal¹,

Jambunathan²,

Mahalingam³

2011

Molecules and Cells

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“…1) [14;15]. In humans, a second gene encodes the nearly identical TIAR protein [16], and at least two alternative spliceoforms exist for both TIA-1 and TIAR [14;15;17]. The Q-rich effecter domain directs TIA-1-associated mRNAs to cytoplasmic stress granules during translational silencing [18], and recruits the U1 spliceosomal component (snRNP) to weak 5′ splice sites during nuclear premRNA splicing [19].…”

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confidence: 99%

Structure of the central RNA recognition motif of human TIA-1 at 1.95 Å resolution

Kumar

Swenson

Benning

et al. 2008

Biochemical and Biophysical Research Communications

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T-cell-restricted intracellular antigen-1 (TIA-1) regulates alternative pre-mRNA splicing in the nucleus, and mRNA translation in the cytoplasm, by recognizing uridine-rich sequences of RNAs. As a step towards understanding of RNA recognition by this regulatory factor, the X-ray structure of the central RNA recognition motif (RRM2) of human TIA-1 is presented at 1.95Å resolution.Comparison with structurally homologous RRM-RNA complexes identifies residues at the RNA interfaces that are conserved in TIA-1-RRM2. The versatile capability of RNP motifs to interact with either proteins or RNA is reinforced by symmetry-related protein-protein interactions mediated by the RNP motifs of TIA-1-RRM2. Importantly, the TIA-1-RRM2 structure reveals the locations of mutations responsible for inhibiting nuclear import. In contrast with previous assumptions, the mutated residues are buried within the hydrophobic interior of the domain, where they would be likely to destabilize the RRM fold rather than directly inhibit RNA binding. KeywordsRRM; RNA binding domain; Pre-mRNA splicing; mRNA translation; TIA-1; TIAR Post-transcriptional mechanisms for regulating gene expression depend on numerous coordinated interactions among RNA sequences and trans-acting protein factors. The RNA binding protein TIA-1 (T-cell-restricted intracellular antigen-1) functions as a posttranscriptional regulator of gene expression by recognizing uridine-rich RNA sites. In the nucleus, TIA-1 regulates alternative splicing of pre-mRNAs, including those encoding fibroblast growth factor receptor-2 (fgfr-2), type II procollagen (col2a1), the cystic fibrosis transmembrane conductance regulator (cftr), and the pro-apoptotic Fas receptor (fas), among others [1;2;3;4;5;6]. In the cytoplasm, TIA-1 regulates mRNA translation [7;8;9;10], and suppresses mRNA translation during environmental stress (reviewed in [11]). The functional importance of TIA-1 is shown by its requirement for viability of DT40 cells [12], and the high rates of embryonic lethality among mice lacking TIA-1 [8;13].*Correspondence E-mail: clara_kielkopf@urmc.rochester.edu; Fax: 585-275-6007. ‡ These authors contributed equally to this work.Publisher's Disclaimer: This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final citable form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. NIH Public Access Materials and Methods Protein purificationThe human TIA-1-RRM2 fragment (residues 94-175) was expressed using the pGEX-6p vector (GE Healthcare). Glutathione-S-transferase (GST) fusion proteins were purified by glutathione affinity, and then the TIA-1 fragment was further purified by cation exchange chromatography following removal of the GST tag....

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“…Overexpression of TIA-1 or TIAR induces apoptosis, whether accomplished by exposure of permeabilized cells to recombinant proteins (1,3), or by infecting cells with an engineered virus (23). During Fas-induced apoptosis, TIA-1 is phosphorylated (24), and TIAR is relocated to the cytoplasm (25).…”

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confidence: 99%

TIA-1 or TIAR Is Required for DT40 Cell Viability

Guiner

Gesnel

Breathnach

2003

Journal of Biological Chemistry

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TIA-1 and TIAR are a pair of related RNA-binding proteins which have been implicated in apoptosis. We show that chicken DT40 cells with both tia-1 alleles and one tiar allele disrupted (tia-1(؊/؊)tiar(؊/؉) cells) are viable. However, their growth and survival in medium containing low serum levels is significantly reduced compared with DT40 cells. The remaining intact tiar allele in tia-1(؊/؊)tiar(؊/؉) cells can only be disrupted if TIA-1 expression is first restored to the cells by transfection of a TIA-1 expression vector. We conclude that DT40 cells require either TIA-1 or TIAR for viability. TIA-1 overexpression in tia-1(؊/؊)tiar(؊/؉) cells leads to a radical drop in TIAR levels, by inducing efficient splicing of two tiar alternative exons carrying in-frame stop codons. In wild-type DT40 cells, tiar transcripts including these exons can also be detected. These transcripts increase significantly in abundance in cycloheximide-treated cells, suggesting that splicing of the exons exposes mRNAs to nonsense-mediated mRNA decay. TIA-1 or TIAR depletion leads to a marked drop in splicing of the exons. The human tiar gene contains a corresponding pair of TIA-1-inducible alternative exons, and we show that there is very high sequence conservation between chickens and humans of the exon pair and parts of the flanking introns. The TIA-1/TIAR responsiveness of these alternative tiar exons is likely to be of physiological importance for controlling TIAR levels.TIA-1 (1 ,2) and the TIA-1-related protein TIAR (3) are a pair of similar, ubiquitous RNA-binding proteins with three RNA recognition motifs (RRMs).1 These proteins fill important functions in both the cytoplasm and the nucleus, as do a number of other multifunctional regulatory proteins (4). In the cytoplasm, TIA-1 and TIAR control translation of some specific mRNAs (5-9) and are active in the general translational arrest mechanism induced by stress (10 -15). TIA-1 and TIAR shuttle between cytoplasm and nucleus, but are predominantly nuclear in most cells studied. In the nucleus, they activate splicing of exons with weak 5Ј-splice sites followed by uridylate-rich stretches (16 -18). TIA-1 and TIAR appear to bind to these stretches (they both bind preferentially to uridylate-rich sequences in vitro, Ref. 19) and assist binding of U1 snRNP to the adjacent 5Ј-splice site. Possible target exons include an fgfr-2 alternative exon (16), a Drosophila msl-2 exon (20), a human fas exon (20), and some alternative human tia-1 and tiar exons containing premature stop codons (21). TIAR and possibly TIA-1 are also involved in replication of the RNA genomes of West Nile virus (22).Overexpression of TIA-1 or TIAR induces apoptosis, whether accomplished by exposure of permeabilized cells to recombinant proteins (1, 3), or by infecting cells with an engineered virus (23). During Fas-induced apoptosis, TIA-1 is phosphorylated (24), and TIAR is relocated to the cytoplasm (25). TIA-1 activates splicing of a fas pre-mRNA exon so as to favor production of a cell death receptor, at the exp...

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Identification and functional characterization of a TIA-1-related nucleolysin.

Cited by 155 publications

References 27 publications

Phylogenetic and Expression Analysis of RNA-binding Proteins with Triple RNA Recognition Motifs in Plants

Phylogenetic and Expression Analysis of RNA-binding Proteins with Triple RNA Recognition Motifs in Plants

Structure of the central RNA recognition motif of human TIA-1 at 1.95 Å resolution

TIA-1 or TIAR Is Required for DT40 Cell Viability

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