Domain architecture of plant eukaryotic translation initiation factor 3 subunit E governs interaction with translational cis-elements to regulatepollen tube growth

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389030%3A_____%2F26%3A00647669" target="_blank" >RIV/61389030:_____/26:00647669 - isvavai.cz</a>

Výsledek na webu

<a href="https://doi.org/10.1093/plcell/koag005" target="_blank" >https://doi.org/10.1093/plcell/koag005</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1093/plcell/koag005" target="_blank" >10.1093/plcell/koag005</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Domain architecture of plant eukaryotic translation initiation factor 3 subunit E governs interaction with translational cis-elements to regulatepollen tube growth

Popis výsledku v původním jazyce

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 eIF3E-dependent 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.

Název v anglickém jazyce

Domain architecture of plant eukaryotic translation initiation factor 3 subunit E governs interaction with translational cis-elements to regulatepollen tube growth

Popis výsledku anglicky

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 eIF3E-dependent 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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10601 - Cell biology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2026

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Plant Cell

ISSN

1040-4651

e-ISSN

1532-298X

Svazek periodika

38

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

26

Strana od-do

koag005

Kód UT WoS článku

001691976200001

EID výsledku v databázi Scopus

2-s2.0-105030415494