Paip2 is localized to active promoters and loaded onto nascent mRNA in Drosophila

We uncovered a nuclear role for human Gle1 in coordinating transcription termination. When nucleocytoplasmic shuttling of Gle1 is disrupted, nascent mRNA transcripts are elongated. Gle1 colocalizes with DDX1, and loss of Gle1 shuttling impairs recruitment of DDX1 to CstF-64 and transcription termination foci, leading to improper pre-mRNA cleavage.

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Elongator Interactions with Nascent mRNA Revealed by RNA Immunoprecipitation

Molecular Cell ◽

10.1016/s1097-2765(04)00239-4 ◽

2004 ◽

Vol 14 (4) ◽

pp. 457-464 ◽

Cited By ~ 103

Author(s):

Christopher Gilbert ◽

Arnold Kristjuhan ◽

G.Sebastiaan Winkler ◽

Jesper Q Svejstrup

Keyword(s):

Rna Immunoprecipitation ◽

Nascent Mrna

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Distinct Functions of the Cap-Binding Complex in Stimulation of Nuclear mRNA Export

Molecular and Cellular Biology ◽

10.1128/mcb.00540-18 ◽

2019 ◽

Vol 39 (8) ◽

Cited By ~ 7

Author(s):

Rwik Sen ◽

Priyanka Barman ◽

Amala Kaja ◽

Jannatul Ferdoush ◽

Shweta Lahudkar ◽

...

Keyword(s):

Saccharomyces Cerevisiae ◽

Protein Level ◽

Mrna Export ◽

Mrna Splicing ◽

Content Type ◽

Cap Binding Complex ◽

Cleavage And Polyadenylation ◽

Nascent Mrna ◽

Stimulation Of ◽

Active Genes

ABSTRACTCap-binding complex (CBC) associates cotranscriptionally with the cap structure at the 5′ end of nascent mRNA to protect it from exonucleolytic degradation. Here, we show that CBC promotes the targeting of an mRNA export adaptor, Yra1 (forming transcription export [TREX] complex with THO and Sub2), to the active genes and enhances mRNA export inSaccharomyces cerevisiae. Likewise, recruitment of Npl3 (an hnRNP involved in mRNA export via formation of export-competent ribonuclear protein complex [RNP]) to the active genes is facilitated by CBC. Thus, CBC enhances targeting of the export factors and promotes mRNA export. Such function of CBC is not mediated via THO and Sub2 of TREX, cleavage and polyadenylation factors, or Sus1 (that regulates mRNA export via transcription export 2 [TREX-2]). However, CBC promotes splicing ofSUS1mRNA and, consequently, Sus1 protein level and mRNA export via TREX-2. Collectively, our results support the hypothesis that CBC promotes recruitment of Yra1 and Npl3 to the active genes, independently of THO, Sub2, or cleavage and polyadenylation factors, and enhances mRNA export via TREX and RNP, respectively, in addition to its role in facilitatingSUS1mRNA splicing to increase mRNA export through TREX-2, revealing distinct stimulatory functions of CBC in mRNA export.

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Functional interaction between the RNA exosome and the sirtuin deacetylase Hst3 maintains transcriptional homeostasis

Genes & Development ◽

10.1101/gad.348923.121 ◽

2021 ◽

Author(s):

Alysia R. Bryll ◽

Craig L. Peterson

Keyword(s):

Rna Synthesis ◽

Optimal Level ◽

Rna Degradation ◽

Eukaryotic Cells ◽

Functional Interaction ◽

Mrna Transcripts ◽

Rna Exosome ◽

Nascent Mrna ◽

Synthesis And Degradation ◽

Global Reduction

Eukaryotic cells maintain an optimal level of mRNAs through unknown mechanisms that balance RNA synthesis and degradation. We found that inactivation of the RNA exosome leads to global reduction of nascent mRNA transcripts, and that this defect is accentuated by loss of deposition of histone variant H2A.Z. We identify the mRNA for the sirtuin deacetylase Hst3 as a key target for the RNA exosome that mediates communication between RNA degradation and transcription machineries. These findings reveal how the RNA exosome and H2A.Z function together to control a deacetylase, ensuring proper levels of transcription in response to changes in RNA degradation.

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Cotranscriptional recruitment of the serine-arginine-rich (SR)-like proteins Gbp2 and Hrb1 to nascent mRNA via the TREX complex

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.0308663100 ◽

2004 ◽

Vol 101 (7) ◽

pp. 1858-1862 ◽

Cited By ~ 84

Author(s):

Ed Hurt ◽

Ming-juan Luo ◽

Susanne Röther ◽

Robin Reed ◽

Katja Sträßer

Keyword(s):

Nascent Mrna

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Tho1, a Novel hnRNP, and Sub2 Provide Alternative Pathways for mRNP Biogenesis in Yeast THO Mutants

Molecular and Cellular Biology ◽

10.1128/mcb.00234-06 ◽

2006 ◽

Vol 26 (12) ◽

pp. 4387-4398 ◽

Cited By ~ 31

Author(s):

Sonia Jimeno ◽

Rosa Luna ◽

María García-Rubio ◽

Andrés Aguilera

Keyword(s):

Nuclear Protein ◽

Rna Binding ◽

Binding Activity ◽

Dependent Manner ◽

Mrna Accumulation ◽

Alternative Pathways ◽

Multicopy Suppressors ◽

Rna Export ◽

Nascent Mrna ◽

Mrnp Biogenesis

ABSTRACT THO is a protein complex that functions in cotranscriptional mRNP formation. Yeast THO1 and SUB2 (Saccharomyces cerevisiae) were identified as multicopy suppressors of the expression defects of the hpr1Δ mutant of THO. Here we show that multicopy THO1 suppresses the mRNA accumulation and export defects and the hyperrecombination phenotype of THO mutants but not those of sub2Δ, thp1Δ, or spt4Δ. Similarly, Sub2 overexpression suppresses the RNA export defect of hpr1Δ. Tho1 is a conserved RNA binding nuclear protein that specifically binds to transcribed chromatin in a THO- and RNA-dependent manner and genetically interacts with the shuttling hnRNP Nab2. The ability of Tho1 to suppress hpr1Δ resides in its C-terminal half, which contains the RNA binding activity and is located after a SAP/SAF (scaffold-associated protein/scaffold-associated factor) domain. Altogether, these results suggest that Tho1 is an hnRNP that, similarly to Sub2, assembles onto the nascent mRNA during transcription and participates in mRNP biogenesis and export. Overexpression of Tho1 or Sub2 may provide alternative ways for mRNP formation and export in the absence of a functional THO complex.

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Conformational Dynamics of the RNA G-Quadruplex and its Effect on Translation Efficiency

Molecules ◽

10.3390/molecules24081613 ◽

2019 ◽

Vol 24 (8) ◽

pp. 1613 ◽

Cited By ~ 7

Author(s):

Tamaki Endoh ◽

Naoki Sugimoto

Keyword(s):

Gene Expression ◽

Conformational Dynamics ◽

Translation Efficiency ◽

Rna Structures ◽

Dominant Effect ◽

Structure Transition ◽

Quadruplex Structure ◽

Metastable Structures ◽

G Quadruplex ◽

Nascent Mrna

During translation, intracellular mRNA folds co-transcriptionally and must refold following the passage of ribosome. The mRNAs can be entrapped in metastable structures during these folding events. In the present study, we evaluated the conformational dynamics of the kinetically favored, metastable, and hairpin-like structure, which disturbs the thermodynamically favored G-quadruplex structure, and its effect on co-transcriptional translation in prokaryotic cells. We found that nascent mRNA forms a metastable hairpin-like structure during co-transcriptional folding instead of the G-quadruplex structure. When the translation progressed co-transcriptionally before the metastable hairpin-like structure transition to the G-quadruplex, function of the G-quadruplex as a roadblock of the ribosome was sequestered. This suggested that kinetically formed RNA structures had a dominant effect on gene expression in prokaryotes. The results of this study indicate that it is critical to consider the conformational dynamics of RNA-folding to understand the contributions of the mRNA structures in controlling gene expression.

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