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Dysregulation of amino acid metabolism upon rapid depletion of cap-binding protein eIF4E

ABSTRACT: Dysregulation of amino acid metabolism upon rapid depletion of cap-binding protein eIF4E

PROVIDER: PRJNA967635 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR24449452.fastq.gz	Fastqsanger.gz
	SRR24449453.fastq.gz	Fastqsanger.gz
	SRR24449454.fastq.gz	Fastqsanger.gz
	SRR24451154.fastq.gz	Fastqsanger.gz
	SRR24449455.fastq.gz	Fastqsanger.gz

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Dysregulation of amino acid metabolism upon rapid depletion of cap-binding protein eIF4E [pcl5_screen]

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 | GSE231757 | GEO

Dysregulation of amino acid metabolism upon rapid depletion of cap-binding protein eIF4E [aro10_screen]

2023-05-09 | GSE231756 | GEO

Dysregulation of amino acid metabolism upon rapid depletion of cap-binding protein eIF4E [RNA-Seq]

2023-05-09 | GSE231758 | GEO

Dysregulation of amino acid metabolism upon rapid depletion of cap-binding protein eIF4E [pcl5_screen]

Project description:Dysregulation of amino acid metabolism upon rapid depletion of cap-binding protein eIF4E [pcl5_screen]

| PRJNA967638 | ENA

Dysregulation of amino acid metabolism upon rapid depletion of cap-binding protein eIF4E [aro10_screen]

Project description:Dysregulation of amino acid metabolism upon rapid depletion of cap-binding protein eIF4E [aro10_screen]

| PRJNA967637 | ENA

Dysregulation of amino acid metabolism upon rapid depletion of cap-binding protein eIF4E [RNA-Seq]

Project description:Dysregulation of amino acid metabolism upon rapid depletion of cap-binding protein eIF4E [RNA-Seq]

| PRJNA967640 | ENA

Dysregulation of amino acid metabolism upon rapid depletion of cap-binding protein eIF4E

Project description:This SuperSeries is composed of the SubSeries listed below.

2023-05-09 | GSE231759 | GEO

Characterization of human malaria parasite Plasmodium falciparum eIF4E homologue and mRNA 5â² cap status

Project description:The mRNA 5â² cap is normally essential for eukaryotic mRNA translation, stabilization and transport and both the cap and eIF4E are important elements of post-transcriptional gene regulation. To further our understanding of mRNA translation in the human malaria parasite Plasmodium falciparum, we have investigated the parasite translation initiation factor eIF4E and its interaction with 5â² capped mRNA. We have purified P. falciparum eIF4E as a recombinant protein and demonstrated that it has canonical mRNA 5â² cap binding activity. We used this protein to purify P. falciparum full-length 5â² capped mRNAs from total parasite RNA. Microarray analysis comparing total and eIF4E-purified 5â² capped mRNAs shows that a subset of 34 features were more than two-fold under-represented in the purified RNA sample, including 19 features representative of nuclear transcripts. The uncapped nuclear transcripts may represent a class of mRNAs targeted for storage and cap removal. Keywords: total RNA vs purified capped mRNA The microarray data were obtained from four hybridizations using RNA from two independent GST-PfeIF4E purifications from separate malaria cultures.

2010-06-10 | E-GEOD-6356 | biostudies-arrayexpress

Discovery of a novel plant eIF4E-binding protein: Conserved Binding of eIF4E 1 (CBE1)

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

Characterization of human malaria parasite Plasmodium falciparum eIF4E homologue and mRNA 5′ cap status

Project description:The mRNA 5′ cap is normally essential for eukaryotic mRNA translation, stabilization and transport and both the cap and eIF4E are important elements of post-transcriptional gene regulation. To further our understanding of mRNA translation in the human malaria parasite Plasmodium falciparum, we have investigated the parasite translation initiation factor eIF4E and its interaction with 5′ capped mRNA. We have purified P. falciparum eIF4E as a recombinant protein and demonstrated that it has canonical mRNA 5′ cap binding activity. We used this protein to purify P. falciparum full-length 5′ capped mRNAs from total parasite RNA. Microarray analysis comparing total and eIF4E-purified 5′ capped mRNAs shows that a subset of 34 features were more than two-fold under-represented in the purified RNA sample, including 19 features representative of nuclear transcripts. The uncapped nuclear transcripts may represent a class of mRNAs targeted for storage and cap removal. Keywords: total RNA vs purified capped mRNA

2007-07-07 | GSE6356 | GEO

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