15 Result(s)
within
Elisa Izaurralde
Membrane Biology
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Article
A novel mode of RBD-protein recognition in the Y14–Mago complex
Y14 and Mago are conserved eukaryotic proteins that associate with spliced mRNAs in the nucleus and remain associated at exon junctions during and after nuclear export. In the cytoplasm, Y14 is involved in mRN...
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Article
Directing mRNA export
A recent study on the RNA-binding protein Npl3p reveals how its direct interaction with the mRNA export receptor Mex67p is regulated by phosphorylation and how this post-translational modification contributes ...
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Article
The structural basis for the interaction between nonsense-mediated mRNA decay factors UPF2 and UPF3
Nonsense-mediated mRNA decay (NMD) is a surveillance mechanism by which eukaryotic cells detect and degrade transcripts containing premature termination codons. Three 'up-frameshift' proteins, UPF1, UPF2 and U...
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Article
Nucleic acid 3′-end recognition by the Argonaute2 PAZ domain
We describe the solution structures of the Argonaute2 PAZ domain bound to RNA and DNA oligonucleotides. The structures reveal a unique mode of single-stranded nucleic acid binding in which the two 3′-terminal ...
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Article
Genome-wide analysis of mRNAs regulated by the THO complex in Drosophila melanogaster
In yeast cells, the THO complex has been implicated in mitotic recombination, transcription elongation and mRNA nuclear export. The stable core of THO consists of Tho2p, Hpr1p, Mft1p and Thp2p. Whether a compl...
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Article
The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin α
Addition of N-acetylglucosamine (GlcNAc) is a ubiquitous form of intracellular glycosylation catalyzed by the conserved O-linked GlcNAc transferase (OGT). OGT contains an N-terminal domain of tetratricopeptide (T...
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Article
GW182 interaction with Argonaute is essential for miRNA-mediated translational repression and mRNA decay
MicroRNAs (miRNAs) silence gene expression by binding 3′ untranslated regions of target mRNAs. Recent studies suggested silencing is achieved through either recruitment of eIF6, which prevents ribosome assembl...
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Article
Structure-function studies of nucleocytoplasmic transport of retroviral genomic RNA by mRNA export factor TAP
The TAP-p15 heterodimer is involved in nuclear export of messenger RNAs. The crystal structure of TAP (RRM + LRR domains) bound to part of the export element found in simian type D retroviral RNAs, together wi...
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Article
A direct interaction between DCP1 and XRN1 couples mRNA decap** to 5′ exonucleolytic degradation
The removal of the mRNA 5′ cap structure by the decap** enzyme DCP2 leads to rapid 5′→3′ mRNA degradation by XRN1, suggesting that the two processes are coordinated. Biochemical and structural analyses now r...
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Article
A role for eIF4AII in microRNA–mediated mRNA silencing
A recent study on the mechanism of microRNA–mediated gene silencing suggests that microRNA–induced silencing complexes inhibit ribosome scanning by recruiting the DEAD-box RNA helicase eIF4AII through an inter...
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Article
Making sense of nonsense
Eukaryotic mRNAs containing nonsense codons are degraded by nonsense-mediated mRNA decay (NMD). In humans, NMD was proposed to act exclusively on newly synthesized mRNA during a 'pioneer round' of translation,...
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Article
Structure and assembly of the NOT module of the human CCR4–NOT complex
The CCR4–NOT deadenylase complex has a crucial role in post-transcriptional mRNA regulation, catalyzing the removal of mRNA poly(A) tails and consequently repressing translation and promoting mRNA degradation....
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Article
An asymmetric PAN3 dimer recruits a single PAN2 exonuclease to mediate mRNA deadenylation and decay
Structural analyses reveal the asymmetric assembly of Neurospora crassa PAN2–PAN3 complex and, along with functional work on the proteins from different species, indicate an essential role for PAN3 in coordinatin...
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Article
Erratum: An asymmetric PAN3 dimer recruits a single PAN2 exonuclease to mediate mRNA deadenylation and decay
Nat. Struct. Mol. Biol. 21, 599–608 (2014); published online 1 June 2014; corrected after print 22 August 2014. In the version of this article initially published, a rotation sign was mistakenly introduced bet...
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Article
Structure of the Dcp2–Dcp1 mRNA-decap** complex in the activated conformation
Crystal structures, along with biochemistry data, capture the active form of the Dcp2 decap** enzyme in complex with Dcp1 and a peptide from Edc1, thus revealing the mechanism of activation by Dcp1 and Edc1 ...
