Dataset Information

Domains architecture and phospho-switches of eIF3e translation subunit control pollen tube growth and morphology

ABSTRACT: The eIF3e subunit form an octameric ribonucleoprotein complex to initiate translation, and its PCI domain engage in the assembly of the proteolytic 26S proteosome supercomplex. These two complexes are central in translation initiation and protein quality surveillance and turnover. However, how eIF3e is structurally regulated remain unknown. Here, using RIPseq approach we revealed that eIF3e co-immunoprecipitate with mRNAs involved in RNA biosynthesis (U3 snRNA12a and ncRNA processing) and cell morphology, and its PCI domain is crucial for regulation of pollen tube pulse growth and eIF3e dissociation post initiation. We show that motifs within eIF3e associated target RNAs can repress or activate translation. Since the PCI domain associate with the proteosome machinery, we show that pharmacological inhibition of the proteosome complex accumulate eIF3e, eIF3eΔPCI and the proteosome lid subunits RPN7/RPN12a to the nucleus and generate nuclear condensates. Importantly, constitutive dephosphorylation of eIF3e revealed antagonistic phosphosites at the PCI domain that balance pollen tube growth and cellular membrane morphology. These findings inform structural features that control eIF3e activities and that antagonistic de-phosphorylation of eIF3e maintain equilibrium of pollen tube growth rate dynamics and membrane structural morphology.

INSTRUMENT(S):

ORGANISM(S): Nicotiana Tabacum (common Tobacco)

SUBMITTER: Petr Pompach

LAB HEAD: Said Hafidh

PROVIDER: PXD048337 | Pride | 2026-04-06

REPOSITORIES: Pride

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Publications

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

Kumar Vinod V Merret Rémy R Carpentier Marie C MC Honys David D Hafidh Said S

The Plant cell 20260201 2

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 l ...[more]

PMID: 41701515

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Project description:As in animals, cell-cell communication plays pivotal role in male-female recognition during plant sexual reproduction. Prelaid peptides secreted from the female reproductive tissues guide pollen tubes towards ovules for fertilization. However, the elaborate mechanisms for this dialogue have remained elusive, particularly from the male perspective. We perform genome-wide quantitative liquid chromatography coupled tandem mass spectrometry of a pistil-stimulated pollen tube secretome and identify 801 pollen tube-secreted proteins. Interestingly, in silico analysis reveals that the pollen tube-secretome is dominated by unconventional-type secreted proteins representing 57% of the total secretome. In support, we show that unconventional-type protein, translationally controlled tumor protein, is secreted to the apoplast. Remarkably, we discover that this protein could be secreted by infiltrating through the initial phases of the conventional secretory pathway and could reach the apoplast via exosomes as demonstrated by co-localization with Oleisin1 exosome marker. We demonstrate that Arabidopsis thaliana translationally controlled tumor protein-knockdown plants have pollen tubes that poorly navigate to the target ovule, and theÂ knocked down allele is poorly transmitted through the male. We show that regulators of the endoplasmic reticulum-trans-golgi network protein secretory pathway control secretion of pollen tube-secreted cysteine-rich proteins, including pollen tube attractants, and are essential for pollen tube growth and guidance, as well as ovule-targeting competence. This work, the first pollen tube secretome study, identifies novel genome-wide pollen tube-secreted proteins with potential function in pollen tube-ovule guidance for sexual reproduction. Functional analysis highlights a potential mechanism for pollen tube unconventional protein secretion and reveals likely regulators of pollen tube protein secretion. The association of pollen tube-secreted proteins with marker proteins shown to be secreted via exosomes in other species suggest secretion via exosomes as a possible mechanism for cell-cell communication between the pollen tube and female reproductive cells. For processed dataset with quantitative information, see Hafidh S, Potesil D, Fila J et al. Genome Bilogy 2016.

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