Discovery of a novel plant eIF4E-binding protein: Conserved Binding of eIF4E 1 (CBE1)
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PROVIDER: PRJNA471077 | ENA |
REPOSITORIES: ENA
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Project description:Regulation of translation initiation is accomplished in diverse eukaryotes through proteins which bind to the mRNA cap-binding protein, eIF4E, and either prevent its association with eIF4G or form repressive mRNPs which exclude the translation machinery. Such mechanisms in plants, and even the presence of eIF4E-interacting proteins outside of eIF4G (and the plant-specific isoform eIFiso4G, which binds eIFiso4E) which operate in a gene regulatory manner are not known. Here we describe the Conserved Binding of eIF4E 1 (CBE1), a plant-specific protein with an evolutionarily conserved eIF4E binding motif. This protein binds eIF4E or eIFiso4E in vitro to form cap-binding complexes, and is found as a constituent of cap-binding complexes in vivo in an eIF4E-dependent manner. Mutants lacking CBE1 show dysregulation of cell cycle related transcripts, accumulating higher levels relative to wild-type plants of mRNAs encoding proteins involved in mitotic processes. These findings support CBE1 as a plant protein with the capability to form cap-binding complexes with the potential for gene regulatory activity.
2018-09-26 | GSE114363 | GEO
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Project description:Discovery of a novel plant eIF4E-binding protein: Conserved Binding of eIF4E 1 (CBE1)
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Project description:Caf20p is one of two Saccharomyces cerevisiae eIF4E binding proteins (4E-BPs) involved in translational control. Both 4E-BPs inhibit translation of a different subset of mRNAs, indicating that 4E-BPs bind specific targets. We used normal and mutated Caf20p to perform RIP-Seq analyses in order to explore the ability of Caf20p for binding mRNAs in 4E-dependent and 4E-independent manners.
2015-09-30 | E-MTAB-2892 | biostudies-arrayexpress
Project description:eIF4E, the major cap-binding protein, has long been considered limiting for translating the mammalian genome. However, the requirement for eIF4E dose at an organismal level remains unexplored. By generating an Eif4e haploinsufficient mouse, we surprisingly found that 50% reduction in eIF4E, while compatible with normal development and global protein synthesis, significantly impeded cellular transformation and tumorigenesis. Genome-wide translational profiling uncovered a translational program induced by oncogenic transformation and revealed a critical role for eIF4E dose specifically in translating a network of mRNAs enriched for a unique 5’UTR signature. In particular, we demonstrate that eIF4E dose is essential for translating mRNAs regulating reactive oxygen species (ROS) that fuel transformation and cancer cell survival in vivo. Therefore, mammalian cells have evolved surplus eIF4E levels that cancer cells hijack to drive a translational program supporting tumorigenesis Total cellular RNA and high MW polysome associated RNA were isolated from matched untransformed and transformed WT and Eif4e+/- MEFs for analysis on Affymetrix Mouse Gene 1.0 ST arrays. The difference in log2 RMA intensity between matched polysomal RNA and total RNA was taken to quantify translational efficiency (TE).
2015-07-01 | E-GEOD-68238 | biostudies-arrayexpress
Project description:eIF4E, the major cap-binding protein, has long been considered limiting for translating the mammalian genome. However, the requirement for eIF4E dose at an organismal level remains unexplored. By generating an Eif4e haploinsufficient mouse, we surprisingly found that 50% reduction in eIF4E, while compatible with normal development and global protein synthesis, significantly impeded cellular transformation and tumorigenesis. Genome-wide translational profiling uncovered a translational program induced by oncogenic transformation and revealed a critical role for eIF4E dose specifically in translating a network of mRNAs enriched for a unique 5’UTR signature. In particular, we demonstrate that eIF4E dose is essential for translating mRNAs regulating reactive oxygen species (ROS) that fuel transformation and cancer cell survival in vivo. Therefore, mammalian cells have evolved surplus eIF4E levels that cancer cells hijack to drive a translational program supporting tumorigenesis
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Project description:Cytoplasmic RNA bound to eIF4E was pulled down from MDA-MB-231 cells to determine the influence of radiation on eIF4E mRNA binding 4 samples were analyzed with 3 biological replicates
2012-06-14 | E-GEOD-36179 | biostudies-arrayexpress
Project description:Cytoplasmic RNA bound to eIF4E was pulled down from MDA-MB-231 cells to determine the influence of radiation on eIF4E mRNA binding
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Project description:Translation is a fundamental step in gene expression that regulates multiple developmental and stress responses. One key step of translation is the association between eIF4E and eIF4G. This process is regulated in different eukaryotes by proteins which bind to eIF4E and block the formation of the eIF4E/eIF4G complex. Here, we report the discovery of CERES, the first functional eIF4E regulator described in plants. CERES is a modular protein that contains a LRR domain and a canonical eIF4E binding site (4E-BS), critical for CERES interaction with eIF4E in planta. CERES/eIF4E interaction excludes eIF4G from the complex. Despite this observation, CERES promotes translation in vivo interacts with eIF4A and with eIF3 in vivo and cosediments with translation initiation complexes in sucrose gradients. Moreover, ceres mutants display a sharp increase of the 80S peak and a reduction of polysome content at specific periods of the diel cycle. Super-resolution ribosome profiling demonstrates that these mutants show a change of translation efficiency of mRNAs related to light response and glucose management. Consistently, these mutants show a hypersensitive response to glucose. These data show that CERES is a “non canonical” translation initiation factor that, through the formation of alternative translation initiation complexes, modulates translation during the light cycle in plants.
2019-12-04 | GSE124290 | GEO
Project description:Protein synthesis is metabolically costly, and the level of translation must match nutrient availability and cellular needs. Overall protein synthesis levels are modulated by regulating translation initiation. The cap-binding protein eIF4E—the earliest contact between mRNAs and the translation machinery—serves as one point of control, but its contributions to mRNA-specific translation regulation remain poorly understood. We acutely depleted eIF4E, which is essential in budding yeast, and observed surprisingly modest effects on cell growth and protein synthesis. Long-lived transcripts were downregulated, likely reflecting accelerated turnover, and the strongest gene-specific effects arose as secondary effects of reduced protein biosynthesis on amino acid pools. Futile cycles of amino acid synthesis and degradation were accompanied by translational activation of GCN4, which is typically induced by amino acid starvation. We further identified translational tuning of PCL5, a negative regulator of Gcn4, that provides a consistent protein-to-mRNA ratio under varying translation environments. This translational control depended in part on a uniquely long poly-(A) tract in the PCL5 5’ UTR and on poly-(A) binding protein. These results highlight the intricate interplay between translation, amino acid homeostasis, and gene regulation and uncover new layers of feedback control in cellular response to stress and nutrient availability.
2023-05-09 | GSE231756 | GEO