The exoribonuclease Dis3L2 defines a novel eukaryotic RNA degradation pathway
The final step of cytoplasmic mRNA degradation proceeds in either a 5′‐3′ direction
catalysed by Xrn1 or in a 3′‐5′ direction catalysed by the exosome. Dis3/Rrp44, an …
catalysed by Xrn1 or in a 3′‐5′ direction catalysed by the exosome. Dis3/Rrp44, an …
Dis3‐like 1: a novel exoribonuclease associated with the human exosome
RHJ Staals, AW Bronkhorst, G Schilders… - The EMBO …, 2010 - embopress.org
The exosome is an exoribonuclease complex involved in the degradation and maturation of
a wide variety of RNAs. The nine‐subunit core of the eukaryotic exosome is catalytically …
a wide variety of RNAs. The nine‐subunit core of the eukaryotic exosome is catalytically …
Exonuclease hDIS3L2 specifies an exosome‐independent 3′‐5′ degradation pathway of human cytoplasmic mRNA
Turnover of mRNA in the cytoplasm of human cells is thought to be redundantly conducted
by the monomeric 5′‐3′ exoribonuclease hXRN1 and the 3′‐5′ exoribonucleolytic …
by the monomeric 5′‐3′ exoribonuclease hXRN1 and the 3′‐5′ exoribonucleolytic …
The human core exosome interacts with differentially localized processive RNases: hDIS3 and hDIS3L
R Tomecki, MS Kristiansen, S Lykke‐Andersen… - The EMBO …, 2010 - embopress.org
The eukaryotic RNA exosome is a ribonucleolytic complex involved in RNA processing and
turnover. It consists of a nine‐subunit catalytically inert core that serves a structural function …
turnover. It consists of a nine‐subunit catalytically inert core that serves a structural function …
The exosome contains domains with specific endoribonuclease, exoribonuclease and cytoplasmic mRNA decay activities
The eukaryotic exosome is a ten-subunit 3′ exoribonucleolytic complex responsible for
many RNA-processing and RNA-degradation reactions. How the exosome accomplishes …
many RNA-processing and RNA-degradation reactions. How the exosome accomplishes …
Genome-wide analysis reveals distinct substrate specificities of Rrp6, Dis3, and core exosome subunits
DL Kiss, ED Andrulis - Rna, 2010 - rnajournal.cshlp.org
The RNA processing exosome complex was originally defined as an evolutionarily
conserved multisubunit complex of ribonucleases responsible for the processing and/or …
conserved multisubunit complex of ribonucleases responsible for the processing and/or …
Evidence for core exosome independent function of the nuclear exoribonuclease Rrp6p
KP Callahan, JS Butler - Nucleic acids research, 2008 - academic.oup.com
The RNA exosome processes and degrades RNAs in archaeal and eukaryotic cells.
Exosomes from yeast and humans contain two active exoribonuclease components, Rrp6p …
Exosomes from yeast and humans contain two active exoribonuclease components, Rrp6p …
[HTML][HTML] Cytoplasmic 5′-3′ exonuclease Xrn1p is also a genome-wide transcription factor in yeast
DA Medina, A Jordán-Pla, G Millán-Zambrano… - Frontiers in …, 2014 - frontiersin.org
The 5′ to 3′ exoribonuclease Xrn1 is a large protein involved in cytoplasmatic mRNA
degradation as a critical component of the major decaysome. Its deletion in the yeast …
degradation as a critical component of the major decaysome. Its deletion in the yeast …
Arabidopsis thaliana exosome subunit AtRrp4p is a hydrolytic 3′→5′ exonuclease containing S1 and KH RNA-binding domains
JA Chekanova, JA Dutko, IS Mian… - Nucleic Acids …, 2002 - academic.oup.com
The exosome, an evolutionarily conserved complex of multiple 3′→ 5′ exoribonucleases,
is responsible for a variety of RNA processing and degradation events in eukaryotes. In this …
is responsible for a variety of RNA processing and degradation events in eukaryotes. In this …
[PDF][PDF] Extensive degradation of RNA precursors by the exosome in wild-type cells
RK Gudipati, Z Xu, A Lebreton, B Séraphin… - Molecular cell, 2012 - cell.com
The exosome is a complex involved in the maturation of rRNA and sn-snoRNA, in the
degradation of short-lived noncoding RNAs, and in the quality control of RNAs produced in …
degradation of short-lived noncoding RNAs, and in the quality control of RNAs produced in …