Dataset Information

The related EIF4G3 and EIF4G4 initiation factors from Leishmania: dissimilar modes of action during translation revealed by a comparative proteomic approach

ABSTRACT: mRNA translation in eukaryotes starts with the binding of the eIF4F complex to its capped 5' end. eIF4F is formed by the joining of its eIF4G and eIF4E subunits, with the former mediating relevant interactions required for translation to proceed. Five eIF4G homologues are found in Leishmania, as part of multiple eIF4F-like complexes, all likely active in translation. Here we performed a large-scale comparative analysis of protein partners associated with two of these eIF4Gs, the related EIF4G3 and EIF4G4. Different transgenic Leishmania infantum cell lines were generated expressing these proteins tagged with a C-terminal HA epitope, each capable of complementing the deletion of the native protein. Proteins associated with the HA-tagged eIF4Gs, after immunoprecipitation with anti-HA beads, were identified through mass spectrometry from three different growth phases: early exponential (24hs), late exponential (48hs) and stationary (96hs). EIF4G3 and EIF4G4 co-precipitated with known and novel protein partners belonging to different functional categories, with some restricted to selected growth phases. The results are thus compatible with the two eIF4Gs likely having related but distinct functions during translation and possibly being targeted by different regulatory mechanisms which are affected by cell growth.

INSTRUMENT(S):

ORGANISM(S): Leishmania Infantum Jpcm5

SUBMITTER: Stéphanny Oliveira

LAB HEAD: Osvaldo Pompílio de Melo Neto

PROVIDER: PXD058985 | Pride | 2026-04-13

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	20221226_111722_Christian_IP124hLdiG3_1.RAW	Raw
	20221226_111722_Christian_IP124hLdiG3_2.RAW	Raw
	20221226_111822_Christian_IP124hLdiG4_1.RAW	Raw
	20221226_111822_Christian_IP124hLdiG4_2.RAW	Raw
	20221226_111922_Christian_IP224hLdiWT_1.RAW	Raw

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The related EIF4G3 and EIF4G4 initiation factors from Leishmania: dissimilar modes of action during translation revealed by a comparative proteomic approach.

Oliveira Stéphanny Sallomé Sousa SSS Melo do Nascimento Larissa L Moura Danielle Maria Nascimento DMN de Souza Reis Christian Robson CR de Melo Neto Osvaldo Pompílio OP

Parasites & vectors 20260304 1

<h4>Background</h4>The start of eukaryotic translation requires recruitment of messenger RNA (mRNA) through the action of the eukaryotic initiation factor 4F (eIF4F) complex. eIF4F is formed by joining of the eIF4G and eIF4E subunits and generally also requires the eIF4A helicase. In Leishmania infantum, five eIF4Gs form multiple eIF4F-like complexes, with those based on the related EIF4G3 and EIF4G4 being active during translation, but with likely nonredundant roles that need to be better defin ...[more]

PMID: 41776682

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Project description:The ability of Leishmania to survive in their insect or mammalian host is dependent upon an ability to sense and adapt to changes in the microenvironment. However, little is known about the molecular mechanisms underlying the parasite response to environmental changes, such as nutrient availability. To elucidate nutrient stress response pathways in Leishmania donovani, we have used purine starvation as the paradigm. The salvage of purines from the host milieu is obligatory for parasite replication; nevertheless, purine-starved parasites can persist in culture without supplementary purine for over 3 months, indicating that the response to purine starvation is robust and engenders parasite survival under conditions of extreme scarcity. To understand metabolic reprogramming during purine starvation we have employed global approaches. Whole proteome comparisons between purine-starved and purine-replete parasites over a 6-48 h span have revealed a temporal and coordinated response to purine starvation. Purine transporters and enzymes involved in acquisition at the cell surface are upregulated within a few hours of purine removal from the media, while other key purine salvage components are upregulated later in the time-course and more modestly.Â After 48 h, the proteome of purine-starved parasites is extensively remodeled and adaptations to purine stress appear tailored to deal with both purine deprivation and general stress. To probe the molecular mechanisms affecting proteome remodeling in response to purine starvation, comparative RNA-seq analyses, qRT-PCR, and luciferase reporter assays were performed on purine-starved versus purine-replete parasites.Â While the regulation of a minority of proteins tracked with changes at the mRNA level, for many regulated proteins it appears that proteome remodeling during purine stress occurs primarily via translational and post-translational mechanisms. One mRNA sample from each of Purine-Starved and Purine-Replete cells were analyzed using SL RNA-Seq methodology