| Title: |
Domain architecture of plant eukaryotic translation initiation factor 3 subunit E governs interaction with translational cis -elements to regulatepollen tube growth |
| Authors: |
Kumar, Vinod; Merret, Rémy; Carpentier, Marie, C; Honys, David; Hafidh, Said |
| Contributors: |
Institute of Experimental Botany of the Czech Academy of Sciences (IEB / CAS); Czech Academy of Sciences Prague (CAS); Univerzita Karlova Praha, Česká republika = Charles University Prague, Czech Republic = Université Charles Prague, Republique tchèque (UK); Institut de Biologie Moléculaire des Plantes (IBMP); Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS); Laboratoire Génome et développement des plantes (LGDP); Institut de Recherche pour le Développement (IRD)-Université de Perpignan Via Domitia (UPVD)-Centre National de la Recherche Scientifique (CNRS); This study is set within the framework of the “Laboratoires d’Excellences (LABEX)” TULIP (ANR-10- LABX-41) and of the “École Universitaire de Recherche (EUR)” TULIP-GS (ANR-18-EURE-0019). We also acknowledge the Structural Mass Spectrometry Core Facility of CIISB, Instruct-CZ Centre, supported by MEYS CR (LM2023042) and European Regional Development Fund-Project “UP CIISB” (no. CZ.02.1.01/0.0/0.0/18_046/0015974).; ANR-10-LABX-0041,TULIP,Towards a Unified theory of biotic Interactions: the roLe of environmental(2010); ANR-18-EURE-0019,TULIP-GSR,The Toulouse-Perpignan(2018) |
| Source: |
ISSN: 1040-4651. |
| Publisher Information: |
CCSD; American Society of Plant Biologists (ASPB) |
| Publication Year: |
2026 |
| Collection: |
Université de Perpignan: HAL |
| Subject Terms: |
[SDV.BV]Life Sciences [q-bio]/Vegetal Biology |
| Description: |
International audience ; An octameric eukaryotic translation initiation factor 3 subunit E (eIF3E) preserves translational homeostasis through selective messenger RNA (mRNA) recognition and ribosome assembly. Yet, the mechanisms by which eIF3E maintains translational equilibriumremain poorly understood. We show here that eIF3E domain architecture and phosphorylation sites (Thr417, Ser421) are conserved across eukaryotes. Deleting the Proteasome-COP9 signalosome-Initiation factor 3 domain (PCI domain) abolished nuclear localization, disrupted eIF3E-eIF3L interaction, and impaired eIF3E dissociation from the polysomes. Affnity RNA immunoprecipitation sequencing of eIF3E::YFP in tobacco pollen tubes identified mRNAs bearing coding-sequence motifs (MC1 to MC3) that co-immunoprecipitate with eIF3E.Using mRNA reporter assay, we reveal that these motifs act in tandem as eIF3Edependent translational repressors and enhancers. AlphaFold3 structural modeling and Förster resonance energy transfer verification indicate that PCI domain deletion or PCI-phosphosite mutagenesis weaken eIF3E-eIF3L interactions and block translational activation of MC2 RNA reporter. We further show thatloss of the PCI domain or PCI-phosphosite mutagenesis misregulate pollen tube growth and membrane organization. Together, our findings underscore eIF3E as a selective regulator of mRNA translation that couplescis-motifrecognition to membrane integrityand pollen tube growth, thereby ensuringplant fertility. |
| Document Type: |
article in journal/newspaper |
| Language: |
English |
| DOI: |
10.1093/plcell/koag005 |
| Availability: |
https://univoak.hal.science/hal-05516327; https://univoak.hal.science/hal-05516327v1/document; https://univoak.hal.science/hal-05516327v1/file/koag005.pdf; https://doi.org/10.1093/plcell/koag005 |
| Rights: |
https://creativecommons.org/licenses/by/4.0/ ; info:eu-repo/semantics/OpenAccess |
| Accession Number: |
edsbas.AC40A5B9 |
| Database: |
BASE |