Department of Microbiology and Physiological Systems
Enzymes and Coenzymes | Fungi | Molecular Biology | Nucleic Acids, Nucleotides, and Nucleosides
A single Dcp1-Dcp2 decapping enzyme targets diverse classes of yeast mRNAs for decapping-dependent 5’ to 3’ decay, but the molecular mechanisms controlling selective mRNA targeting by the enzyme remain elusive. Through extensive genetic analyses we uncover cis-regulatory elements in the Dcp2 C-terminal domain that control selective targeting of the decapping enzyme by forming distinct decapping complexes. Two Upf1-binding motifs target the decapping enzyme to NMD substrates, and a single Edc3-binding motif targets both Edc3 and Dhh1 substrates. Pat1-binding leucine-rich motifs target Edc3 and Dhh1 substrates under selective conditions. Although it functions as a unique targeting component of specific complexes, Edc3 is a common component of multiple complexes. Xrn1 also has a specific Dcp2 binding site, allowing it to be directly recruited to decapping complexes. Collectively, our results demonstrate that Upf1, Edc3, and Pat1 function as regulatory subunits of the holo-decapping enzyme, controlling both its targeting specificity and enzymatic activation.
mRNA decay, NMD, Dcp1, Dcp2, Edc3, Upf1, Pat1, Xrn1
Rights and Permissions
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
DOI of Published Version
bioRxiv 2021.10.01.462794; doi: https://doi.org/10.1101/2021.10.01.462794. Link to preprint on bioRxiv.
He F, Wu C, Jacobson AS. (2021). Dcp2 C-terminal Cis-Binding Elements Control Selective Targeting of the Decapping Enzyme by Forming Distinct Decapping Complexes [preprint]. University of Massachusetts Medical School Faculty Publications. https://doi.org/10.1101/2021.10.01.462794. Retrieved from https://escholarship.umassmed.edu/faculty_pubs/2102
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.