TFIP11 Interacts with mDEAH9, an RNA Helicase Involved in Spliceosome Disassembly

Wen, Xin; Tannukit, Sissada; Paine, Michael L.

doi:10.3390/ijms9112105

Cited by 30 publications

(37 citation statements)

References 13 publications

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“…The yeast homologue of TFIP11, Ntr1 (Nineteen-complex related protein 1), which shows ~ 30% amino acid similarity with mammalian TFIP11s, has been shown to interact directly with Prp43, an ATP-dependent RNA helicase [7,8,9,10], thereby recruiting Prp43 to the spliceosome, a required step for the release of the lariat-intron and spliceosome disassembly in yeast [11]. Similar functional roles for TFIP11 and DHX15, the mammalian homologue of Prp43, have been described whereby TFIP11 within the U4/U6.U5 snRNP complex recruits DHX15 from the nucleoplasm, to enable the release of the lariat-intron during late-stage pre-mRNA splicing [12,13,14]. Failure of TFIP11 to recruit and interact with DHX15 results in the failure of the splicing complex to disassemble and release U2, U5, and U6 snRNPs, leading to the accumulation of post-splicing intron complexes and compromising cell behavior and survival [13].…”

Section: Introductionmentioning

confidence: 98%

“…Failure of TFIP11 to recruit and interact with DHX15 results in the failure of the splicing complex to disassemble and release U2, U5, and U6 snRNPs, leading to the accumulation of post-splicing intron complexes and compromising cell behavior and survival [13]. TFIP11 contains a G-patch, which is a signature motif of many RNA-processing proteins [3,12,15]. Recent work suggests that the G-patch of TFIP11 is necessary for TFIP11-DHX15 interaction [13].…”

Section: Introductionmentioning

confidence: 99%

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Identification of a novel nuclear localization signal and speckle-targeting sequence of tuftelin-interacting protein 11, a splicing factor involved in spliceosome disassembly

Tannukit

Crabb

Hertel

et al. 2009

Biochemical and Biophysical Research Communications

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Tuftelin-interacting protein 11 (TFIP11) is a protein component of the spliceosome complex that promotes the release of the lariat-intron during late-stage splicing through a direct recruitment and interaction with DHX15/PRP43. Expression of TFIP11 is essential for cell and organismal survival. TFIP11 contains a G-patch domain, a signature motif of RNA-processing proteins that is responsible for TFIP11-DHX15 interactions. No other functional domains within TFIP11 have been described. TFIP11 is localized to distinct speckled regions within the cell nucleus, although excluded from the nucleolus. In this study sequential C-terminal deletions and mutational analyses have identified two novel protein elements in mouse TFIP11. The first domain covers amino acids 701-706 (VKDKFN) and is an atypical nuclear localization signal (NLS). The second domain is contained within amino acids 711-735 and defines TFIP11's distinct speckled nuclear localization. The identification of a novel TFIP11 nuclear speckle targeting sequence (TFIP11-STS) suggests that this domain directly interacts with additional spliceosomal components. These data help define the mechanism of nuclear/ nuclear speckle localization of the splicing factor TFIP11, with implications for it's function.

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Section: Introductionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

Identification of a novel nuclear localization signal and speckle-targeting sequence of tuftelin-interacting protein 11, a splicing factor involved in spliceosome disassembly

Tannukit

Crabb

Hertel

et al. 2009

Biochemical and Biophysical Research Communications

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“…The yeast homolog of DHX15 may recruit Prp43 to remove the lariat-intron in late-stage RNA splicing activity and play a critical role in modulating pre-mRNA splicing (34). However, the function of DHX15 in the innate immune system is unknown.…”

Section: Introductionmentioning

confidence: 99%

DHX15 Senses Double-Stranded RNA in Myeloid Dendritic Cells

Lü

Weng

et al. 2014

The Journal of Immunology

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Many members of the DEXD/H-box helicase family play important roles in the innate immune system against viral infection. We, therefore, isolated double-stranded RNA (dsRNA) complex in myeloid dendritic cells (mDCs). We found that DHX15, a DEXDc helicase family member, is one of the components of this complex. Knockdown of DHX15 expression by short hairpin RNA efficiently reduced the ability of mDCs to produce interferon beta (IFN-β), IL-6 and TNF-α in response to dsRNA and RNA virus. DHX15 specifically bound poly I:C via its HELICc domain. DHX15 interacted with MAVS and formed a complex following stimulation with poly I:C. The N-terminal domain containing a DEXDc motif in DHX15 bound the C-terminus of MAVS. DHX15 is required to activate IRF3 phosphorylation, as well as NF-κB and MAPK signaling during RNA virus infection. We, therefore, identified DHX15 as a new RNA virus sensor mediated by MAVS to activate the immune responses to RNA.

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“…The yeast Prp43 protein and its mammalian homolog DHX15 also act to dislodge the intron from the postcatalytic spliceosome and to recycle essential snRNP factors for use in subsequent rounds of splicing (Arenas and Abelson 1997;Martin et al 2002;Tsai et al 2005;Wen et al 2008;Fourmann et al 2013). Prp43 activity contributes to the maintenance of spliceosome integrity because reduced Prp43 function promotes the use of structurally aberrant spliceosomes and the splicing of suboptimal premRNA substrates (Pandit et al 2006;Koodathingal et al 2010;Mayas et al 2010;Chen et al 2013).…”

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confidence: 99%

Limited Portability of G-Patch Domains in Regulators of the Prp43 RNA Helicase Required for Pre-mRNA Splicing and Ribosomal RNA Maturation in Saccharomyces cerevisiae

Banerjee¹,

McDaniel²,

Rymond

2015

Genetics

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The Prp43 DExD/H-box protein is required for progression of the biochemically distinct pre-messenger RNA and ribosomal RNA (rRNA) maturation pathways. In Saccharomyces cerevisiae, the Spp382/Ntr1, Sqs1/Pfa1, and Pxr1/Gno1 proteins are implicated as cofactors necessary for Prp43 helicase activation during spliceosome dissociation (Spp382) and rRNA processing (Sqs1 and Pxr1). While otherwise dissimilar in primary sequence, these Prp43-binding proteins each contain a short glycine-rich G-patch motif required for function and thought to act in protein or nucleic acid recognition. Here yeast two-hybrid, domain-swap, and site-directed mutagenesis approaches are used to investigate G-patch domain activity and portability. Our results reveal that the Spp382, Sqs1, and Pxr1 G-patches differ in Prp43 two-hybrid response and in the ability to reconstitute the Spp382 and Pxr1 RNA processing factors. G-patch protein reconstitution did not correlate with the apparent strength of the Prp43 two-hybrid response, suggesting that this domain has function beyond that of a Prp43 tether. Indeed, while critical for Pxr1 activity, the Pxr1 G-patch appears to contribute little to the yeast two-hybrid interaction. Conversely, deletion of the primary Prp43 binding site within Pxr1 (amino acids 102-149) does not impede rRNA processing but affects small nucleolar RNA (snoRNA) biogenesis, resulting in the accumulation of slightly extended forms of select snoRNAs, a phenotype unexpectedly shared by the prp43 loss-of-function mutant. These and related observations reveal differences in how the Spp382, Sqs1, and Pxr1 proteins interact with Prp43 and provide evidence linking G-patch identity with pathway-specific DExD/H-box helicase activity.KEYWORDS Saccharomyces cerevisiae; spliceosome; rRNA processing; DExD/H-box protein; pre-mRNA splicing N UMEROUS genome-wide interaction and gene expression studies identify ribosome biogenesis as a central integrative feature of Saccharomyces cerevisiae metabolism (see, e.g ., Mnaimneh et al. 2004;Davierwala et al. 2005;Gavin et al. 2006;Collins et al. 2007;Hu et al. 2007;Magtanong et al. 2011). In rapidly dividing organisms such as this budding yeast, ribosomal RNAs (rRNAs) make up the lion's share of cellular nucleic acid by mass, while ribosomal protein transcripts can account for more than half the transcribed messenger RNA (mRNA). Because ribosome biogenesis is so energetically costly, eukaryotes have evolved multiple means to regulate rRNA and ribosomal protein production in response to changes in cellular demand and surveillance systems to remove aberrant ribosomal protein complexes formed during assembly or after environmental insult (Jorgensen et al. 2002;Fingerman et al. 2003; FromontRacine et al. 2003;Jorgensen et al. 2004;Marion et al. 2004;Henras et al. 2008;Kressler et al. 2010;Lafontaine 2010). The coordination of pre-mRNA processing with ribosome biogenesis is especially relevant in the intron-poor environment of the yeast genome, where the highly expressed ribosomal protein transcr...

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TFIP11 Interacts with mDEAH9, an RNA Helicase Involved in Spliceosome Disassembly

Cited by 30 publications

References 13 publications

Identification of a novel nuclear localization signal and speckle-targeting sequence of tuftelin-interacting protein 11, a splicing factor involved in spliceosome disassembly

Identification of a novel nuclear localization signal and speckle-targeting sequence of tuftelin-interacting protein 11, a splicing factor involved in spliceosome disassembly

DHX15 Senses Double-Stranded RNA in Myeloid Dendritic Cells

Limited Portability of G-Patch Domains in Regulators of the Prp43 RNA Helicase Required for Pre-mRNA Splicing and Ribosomal RNA Maturation in Saccharomyces cerevisiae

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