Identification and Analysis of the Interaction between Edc3 and Dcp2 in Saccharomyces cerevisiae [PDF]
Cap hydrolysis is a critical control point in the life of eukaryotic mRNAs and is catalyzed by the evolutionarily conserved Dcp1-Dcp2 complex. In Saccharomyces cerevisiae, decapping is modulated by several factors, including the Lsm family protein Edc3, which directly binds to Dcp2.
Yuriko, Harigaya +4 more
openaire +2 more sources
Control of mRNA decapping by Dcp2: An open and shut case? [PDF]
mRNA decapping by Dcp2 is a critical step in several major eukaryotic mRNA decay pathways. Dcp2 forms the catalytic core of a mRNP that is configured for processing diverse substrates by pathway-specific activators. Here we elaborate a model of catalysis by Dcp2 which posits that activity is controlled by a conformational equilibrium between an open ...
Stephen N, Floor +2 more
openaire +2 more sources
METTL3 promotes chemoresistance in small cell lung cancer by inducing mitophagy
Background Small cell lung cancer (SCLC) is the most aggressive subtype of lung cancer. Although most patients are initially sensitive to first-line combination chemotherapy with cisplatin and etoposide, chemotherapy drug resistance easily develops and ...
Yueqin Sun +7 more
doaj +1 more source
The C-terminal domain from S. cerevisiae Pat1 displays two conserved regions involved in decapping factor recruitment. [PDF]
Eukaryotic mRNA decay is a highly regulated process allowing cells to rapidly modulate protein production in response to internal and environmental cues.
Zaineb Fourati +11 more
doaj +1 more source
Transcript-Specific Decapping and Regulated Stability by the Human Dcp2 Decapping Protein [PDF]
mRNA decapping is a critical step in the control of mRNA stability and gene expression and is carried out by the Dcp2 decapping enzyme. Dcp2 is an RNA binding protein that must bind RNA in order to recognize the cap for hydrolysis. We demonstrate that human Dcp2 (hDcp2) preferentially binds to a subset of mRNAs and identify sequences at the 5' terminus
You, Li +2 more
openaire +2 more sources
Functions of Dcp2 and Ski7 In Mrna Degradation [PDF]
Posttranscriptional gene regulation is essential to maintain gene expression fidelity. This is partially achieved by mRNA decay. When no longer required, mRNA is degraded by two alternative pathways.
van Hoof, Ambro, Kim, Minseon
core +1 more source
Interdomain dynamics and coactivation of the mRNA decapping enzyme Dcp2 are mediated by a gatekeeper tryptophan [PDF]
Conformational dynamics in bilobed enzymes can be used to regulate their activity. One such enzyme, the eukaryotic decapping enzyme Dcp2, controls the half-life of mRNA by cleaving the 5′ cap structure, which exposes a monophosphate that is efficiently degraded by exonucleases.
Stephen N, Floor +2 more
openaire +2 more sources
Geminivirus Activates ASYMMETRIC LEAVES 2 to Accelerate Cytoplasmic DCP2-Mediated mRNA Turnover and Weakens RNA Silencing in Arabidopsis. [PDF]
Aberrant viral RNAs produced in infected plant cells serve as templates for the synthesis of dsRNAs. The derived virus-related small interfering RNAs (siRNA) mediate cleavage of viral RNAs by post-transcriptional gene silencing (PTGS), thus blocking ...
Jian Ye +8 more
doaj +1 more source
Competition between Decapping Complex Formation and Ubiquitin-Mediated Proteasomal Degradation Controls Human Dcp2 Decapping Activity [PDF]
mRNA decapping is a central step in eukaryotic mRNA decay that simultaneously shuts down translation initiation and activates mRNA degradation. A major complex responsible for decapping consists of the decapping enzyme Dcp2 in association with decapping ...
Erickson, Stacy L +6 more
core +1 more source
A non-canonical role for the EDC4 decapping factor in regulating MARF1-mediated mRNA decay
EDC4 is a core component of processing (P)-bodies that binds the DCP2 decapping enzyme and stimulates mRNA decay. EDC4 also interacts with mammalian MARF1, a recently identified endoribonuclease that promotes oogenesis and contains a number of RNA ...
William R Brothers +3 more
doaj +1 more source

