Results 11 to 20 of about 3,123 (186)

Pby1 is a direct partner of the Dcp2 decapping enzyme [PDF]

Nucleic Acids Research, 2020
International audienceMost eukaryotic mRNAs harbor a characteristic 5 m 7 GpppN cap that promotes pre-mRNA splicing, mRNA nucleocytoplasmic transport and translation while also protecting mRNAs from exonucleolytic attacks.
Ulryck, Nathalie, Graille, Marc, Cosson, Loreline, Séraphin, Bertrand, Back, Régis, Gaudon-Plesse, Claudine, Charenton, Clément   +6 more
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Structural basis of dcp2 recognition and activation by dcp1 [PDF]

Molecular Cell, 2008
A critical step in mRNA degradation is the removal of the 5' cap structure, which is catalyzed by the Dcp1-Dcp2 complex. The crystal structure of an S.
Decker, C. J., Chen, N., Parker, R., She, M., Song, H., Svergun, D. I., Round, A., Muhlrad, D.   +7 more
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Intrinsically disordered regions of tristetraprolin and DCP2 directly interact to mediate decay of ARE-mRNA [PDF]

Nucleic Acids Research, 2022
The RNA-binding protein tristetraprolin (TTP) is a potent activator of mRNA decay, specifically for transcripts bearing AU-rich elements (AREs) in their 3′-untranslated regions.
Maciej, Vincent D., Maciej, Vincent D, Mallick, Megha, Dittmers, Theresa, Mateva, Nevena, Chakrabarti, Sutapa, Urlaub, Henning, Schwarz, Juliane   +7 more
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Role of DCP1-DCP2 complex regulated by viral and host microRNAs in DNA virus infection [PDF]

Fish & Shellfish Immunology, 2018
The DCP1-DCP2 complex can regulate the animal antiviral immunity by the decapping of retrovirus RNAs and the suppression of RNAi pathway. However, the influence of DCP1-DCP2 complex on DNA virus infection and the regulation of DCP1-DCP2 complex by ...
Yuechao Sun, Xiaobo Zhang
core   +3 more sources

The structural basis of Edc3- and Scd6-mediated activation of the Dcp1:Dcp2 mRNA decapping complex [PDF]

The EMBO Journal, 2011
The Dcp1:Dcp2 decapping complex catalyses the removal of the mRNA 5' cap structure. Activator proteins, including Edc3 (enhancer of decapping 3), modulate its activity.
Izaurralde, E., Fromm, S. A., Izaurralde, Elisa, Vincent Truffault, Truffault, Vincent, Simon A Fromm, Kamenz, Julia, Braun, J. E., Braun, J., Hoffmann, N., Sprangers, R., Kamenz, J., Joerg E Braun, Hoffmann, Niklas A., Julia Kamenz, Truffault, V., Fromm, Simon A., Elisa Izaurralde, Niklas A Hoffmann, Fromm, S., Sprangers, Remco, Braun, Jeorg E., Hoffmann, N. A., Remco Sprangers, Braun, Jörg Eberhard   +24 more
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A split active site couples cap recognition by Dcp2 to activation [PDF]

Nature Structural & Molecular Biology, 2010
Decapping by Dcp2 is an essential step in 5'-to-3' mRNA decay. In yeast, decapping requires an open-to-closed transition in Dcp2, though the link between closure and catalysis remains elusive.
Gross, John D, Hernandez, Gail A, John D Gross, Stephen N Floor, Gail A Hernandez, Floor, Stephen N, Brittnee N Jones, Jones, Brittnee N   +7 more
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Disruption of Dcp1 leads to a Dcp2‐dependent aberrant ribosome profiles in Aspergillus nidulans [PDF]

Molecular Microbiology, 2023
There are multiple RNA degradation mechanisms in eukaryotes, key among these is mRNA decapping, which requires the Dcp1‐Dcp2 complex. Decapping is involved in various processes including nonsense‐mediated decay (NMD), a process by which aberrant ...
Mark X. Caddick, Caddick, MX, Caddick, Mark X., Matthew T. F. Lamaudière, Sean R. Connell, Connell, SR, Bharudin, I, Bharudin, Izwan, Morozov, IY, Connell, Sean R., Izwan Bharudin, Morozov, Igor Y.; id_orcid, Igor Y. Morozov, Lamaudière, MTF, Lamaudière, Matthew T. F.   +14 more
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Dcp1 links coactivators of mRNA decapping to Dcp2 by proline recognition [PDF]

RNA, 2010
Cap hydrolysis is a critical step in several eukaryotic mRNA decay pathways and is carried out by the evolutionarily conserved decapping complex containing Dcp2 at the catalytic core. In yeast, Dcp1 is an essential activator of decapping and coactivators
John D. Gross, Freund, Christian, Christian Freund, Borja, Mark S., Mark S. Borja, Kirill Piotukh, Piotukh, Kirill, Gross, John D.   +7 more
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Active Site Conformational Dynamics Are Coupled to Catalysis in the mRNA Decapping Enzyme Dcp2 [PDF]

Structure, 2013
SummaryRemoval of the 5′ cap structure by Dcp2 is a major step in several 5′–3′ mRNA decay pathways. The activity of Dcp2 is enhanced by Dcp1 and bound coactivators, yet the details of how these interactions are linked to chemistry are poorly understood.
Aglietti, Robin A., McClendon, Chris L., Jacobson, Matthew P, Gross, John D, Aglietti, Robin A, Floor, Stephen N., McClendon, Chris L, Floor, Stephen N, Jacobson, Matthew P., Gross, John D.   +9 more
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Decapping factor Dcp2 controls mRNA abundance and translation to adjust metabolism and filamentation to nutrient availability

eLife, 2023
Degradation of most yeast mRNAs involves decapping by Dcp1/Dcp2. DEAD-box protein Dhh1 has been implicated as an activator of decapping, in coupling codon non-optimality to enhanced degradation, and as a translational repressor, but its functions in ...
Anil Kumar Vijjamarri, Xiao Niu, Matthew D Vandermeulen, Chisom Onu, Fan Zhang, Hongfang Qiu, Neha Gupta, Swati Gaikwad, Miriam L Greenberg, Paul J Cullen, Zhenguo Lin, Alan G Hinnebusch   +11 more
doaj   +2 more sources