Dcp2 C-terminal Cis-Binding Elements Control Selective Targeting of the Decapping Enzyme by Forming Distinct Decapping Complexes [preprint]
dc.contributor.author | He, Feng | |
dc.contributor.author | Wu, Chan | |
dc.contributor.author | Jacobson, Allan | |
dc.date | 2022-08-11T08:08:28.000 | |
dc.date.accessioned | 2022-08-23T15:56:07Z | |
dc.date.available | 2022-08-23T15:56:07Z | |
dc.date.issued | 2021-10-01 | |
dc.date.submitted | 2021-11-29 | |
dc.identifier.citation | <p>bioRxiv 2021.10.01.462794; doi: https://doi.org/10.1101/2021.10.01.462794. <a href="https://doi.org/10.1101/2021.10.01.462794" target="_blank" title="view preprint in biorxiv">Link to preprint on bioRxiv.</a></p> | |
dc.identifier.doi | 10.1101/2021.10.01.462794 | |
dc.identifier.uri | http://hdl.handle.net/20.500.14038/29898 | |
dc.description | <p>This article is a preprint. Preprints are preliminary reports of work that have not been certified by peer review.</p> | |
dc.description.abstract | 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. | |
dc.language.iso | en_US | |
dc.relation | Now published in eLife doi: 10.7554/eLife.74410 | |
dc.rights | 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. | |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | |
dc.subject | mRNA decay | |
dc.subject | NMD | |
dc.subject | Dcp1 | |
dc.subject | Dcp2 | |
dc.subject | Edc3 | |
dc.subject | Upf1 | |
dc.subject | Pat1 | |
dc.subject | Xrn1 | |
dc.subject | Enzymes and Coenzymes | |
dc.subject | Fungi | |
dc.subject | Molecular Biology | |
dc.subject | Nucleic Acids, Nucleotides, and Nucleosides | |
dc.title | Dcp2 C-terminal Cis-Binding Elements Control Selective Targeting of the Decapping Enzyme by Forming Distinct Decapping Complexes [preprint] | |
dc.type | Preprint | |
dc.source.journaltitle | bioRxiv | |
dc.identifier.legacyfulltext | https://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=3116&context=faculty_pubs&unstamped=1 | |
dc.identifier.legacycoverpage | https://escholarship.umassmed.edu/faculty_pubs/2102 | |
dc.identifier.contextkey | 26339224 | |
refterms.dateFOA | 2022-08-23T15:56:07Z | |
html.description.abstract | <p>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 <em>cis</em>-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.</p> | |
dc.identifier.submissionpath | faculty_pubs/2102 | |
dc.contributor.department | Department of Microbiology and Physiological Systems |