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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Exoribonuclease 1

exoribonuclease, eri-1, 3'-exoribonuclease
Top mentioned proteins: CAN, caspase-3, XRN1, POLYMERASE, STEP
Papers on exoribonuclease
The ribonuclease polynucleotide phosphorylase can interact with small regulatory RNAs in both protective and degradative modes.
De Lay et al., Cambridge, United Kingdom. In Rna, Feb 2016
Many of the actions of these nucleic acids are mediated by well-characterized chaperones such as the Hfq protein, but genetic screens have also recently identified the 3'-to-5' exoribonuclease polynucleotide phosphorylase (PNPase) as an unexpected stabilizer and facilitator of sRNAs in vivo.
Regulation and functions of bacterial PNPase.
Dehò et al., Milano, Italy. In Wiley Interdiscip Rev Rna, Feb 2016
UNASSIGNED: Polynucleotide phosphorylase (PNPase) is an exoribonuclease that catalyzes the processive phosphorolytic degradation of RNA from the 3'-end.
Molecular recognition of mRNA 5' cap by 3' poly(a)-specific ribonuclease (PARN) differs from interactions known for other cap-binding proteins.
Virtanen et al., Warsaw, Poland. In Biochim Biophys Acta, Feb 2016
Poly(A)-specific ribonuclease (PARN) is a dimeric exoribonuclease that efficiently degrades mRNA 3' poly(A) tails while also simultaneously interacting with the mRNA 5' cap.
P-TEFb regulation of transcription termination factor Xrn2 revealed by a chemical genetic screen for Cdk9 substrates.
Fisher et al., New York City, United States. In Genes Dev, Feb 2016
Among the RNA processing factors phosphorylated by Cdk9 was the 5'-to-3' "torpedo" exoribonuclease Xrn2, required in transcription termination by Pol II, which we validated as a bona fide P-TEFb substrate in vivo and in vitro.
Antagonistic roles between Nibbler and Hen1 modulate piRNA 3' ends in Drosophila.
Liu et al., Shanghai, China. In Development, Jan 2016
Here, we identify a protein-protein interaction between Nibbler (Nbr), a 3'-to-5' exoribonuclease and Piwi, linking Nbr activity with piRNA pathways.
An intriguing RNA species-perspectives of circularized RNA.
Ni et al., Shanghai, China. In Protein Cell, Dec 2015
CircRNAs have a more stable molecular structure that can resist to exoribonuclease comparing to those linear ones, and their molecular functions include microRNA sponge, regulatory roles in transcription, mRNA traps that compete with linear splicing, templates for translation and possibly other presently unknown roles.
Standing your ground to exoribonucleases: Function of Flavivirus long non-coding RNAs.
Wilusz et al., Fort Collins, United States. In Virus Res, Oct 2015
These non-coding RNAs, which are called subgenomic flavivirus RNAs (sfRNAs) or Xrn1-resistant RNAs (xrRNAs), are stable decay intermediates generated from the viral genomic RNA through the stalling of the cellular exoribonuclease Xrn1 at highly structured regions.
Surprises in the 3'-end: 'U' can decide too!
Arraiano et al., Lisbon, Portugal. In Febs J, Sep 2015
Namely, Dis3L2 is a 3'-5' exoribonuclease from the RNase II/RNB family that has been shown to act preferentially on oligo(U)-tailed transcripts.
Exome sequencing links mutations in PARN and RTEL1 with familial pulmonary fibrosis and telomere shortening.
Garcia et al., Dallas, United States. In Nat Genet, May 2015
Gene burden analysis comparing 78 European cases and 2,816 controls implicated PARN, an exoribonuclease with no previous connection to telomere biology or disease, with five new heterozygous damaging mutations in unrelated cases and none in controls (P = 1.3 × 10(-8)); mutations were shared by all affected relatives (odds in favor of linkage = 4,096:1).
The 3' to 5' Exoribonuclease DIS3: From Structure and Mechanisms to Biological Functions and Role in Human Disease.
Newbury et al., Brighton, United Kingdom. In Biomolecules, 2014
DIS3 is a conserved exoribonuclease and catalytic subunit of the exosome, a protein complex involved in the 3' to 5' degradation and processing of both nuclear and cytoplasmic RNA species.
Promotion of Bamboo Mosaic Virus Accumulation in Nicotiana benthamiana by 5'→3' Exonuclease NbXRN4.
Meng et al., T'ai-chung-shih, Taiwan. In Front Microbiol, 2014
Among them, the cytoplasmic exoribonuclease NbXRN4 particularly caught our attention.
Exonuclease-mediated degradation of nascent RNA silences genes linked to severe malaria.
Scherf et al., Shanghai, China. In Nature, 2014
We identify a novel chromatin-associated exoribonuclease, termed PfRNase II, that controls the silencing of upsA var genes by marking their transcription start site and intron-promoter regions leading to short-lived cryptic RNA.
Structure of an Rrp6-RNA exosome complex bound to poly(A) RNA.
Lima et al., New York City, United States. In Nature, 2014
The eukaryotic RNA exosome processes and degrades RNA by directing substrates to the distributive or processive 3' to 5' exoribonuclease activities of Rrp6 or Rrp44, respectively.
The yeast ski complex: crystal structure and RNA channeling to the exosome complex.
Conti et al., München, Germany. In Cell, 2013
Biochemical data suggest that the Ski complex can thread RNAs directly to the exosome, coupling the helicase and the exoribonuclease through a continuous RNA channel.
An RNA degradation machine sculpted by Ro autoantigen and noncoding RNA.
Wolin et al., New Haven, United States. In Cell, 2013
We report that Rsr and the exoribonuclease polynucleotide phosphorylase (PNPase) form an RNA degradation machine that is scaffolded by Y RNA.
Eri1 regulates microRNA homeostasis and mouse lymphocyte development and antiviral function.
Ansel et al., San Francisco, United States. In Blood, 2012
Mouse Eri1 regulates miRNA homeostasis in lymphocytes and is required for normal NK-cell development and antiviral immunity.
Mouse Eri1 interacts with the ribosome and catalyzes 5.8S rRNA processing.
Heissmeyer et al., Boston, United States. In Nat Struct Mol Biol, 2008
Findings indicate that Eri1 catalyzes the final trimming step in 5.8S rRNA processing, functionally and spatially connecting this regulator of RNAi with the basal translation machinery.
Characterization of 3'hExo, a 3' exonuclease specifically interacting with the 3' end of histone mRNA.
Dominski et al., Chapel Hill, United States. In J Biol Chem, 2006
3'hExo is a 3' exonuclease specifically interacting with the 3' end of histone mRNA
High doses of siRNAs induce eri-1 and adar-1 gene expression and reduce the efficiency of RNA interference in the mouse.
Huang et al., Shanghai, China. In Biochem J, 2005
The roles of meri-1 (mouse enhanced RNAi) and adar1 in the regulation of RNA interference are reported.
Crystallographic structure of the nuclease domain of 3'hExo, a DEDDh family member, bound to rAMP.
Patel et al., New York City, United States. In J Mol Biol, 2004
Data describe the structure of the nuclease domain of 3'-5'-exoribonuclease (3'hExo) complexed with rAMP in the presence of magnesium at 1.6 A resolution.
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