Homo sapiens
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA331206 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR3951704.fastq.gz | Fastqsanger.gz | |||
| SRR3951705.fastq.gz | Fastqsanger.gz | |||
| SRR3951706.fastq.gz | Fastqsanger.gz | |||
| SRR3951707.fastq.gz | Fastqsanger.gz |
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Project description:hCLE/C14orf166/RTRAF, DDX1 and HSPC117 are components of cytoplasmic mRNA-transporting granules kinesin-associated in dendrites. They have also been found in cytoplasmic ribosome-containing RNA granules that transport specific mRNAs halted for translation until specific neuronal signals renders them accessible to the translation machinery. hCLE associates to DDX1, HSPC117 and FAM98B in HEK293T cells and all four proteins bind to cap analog-containing resins. Competition and elution experiments indicate that binding of hCLE complex to cap resins is independent of eIF4E; the cap-binding factor needed for translation. Purified hCLE free of its associated proteins binds cap with low affinity suggesting that its interacting proteins modulate its cap association. hCLE silencing reduces hCLE accumulation and that of its interacting proteins and decreases mRNA translation. hCLE-associated RNAs have been isolated and sequenced; RNAs involved in mRNA translation are specifically associated. The data suggest a positive role of hCLE complex modulating mRNA translation.
2019-02-18 | GSE84824 | GEO
Project description:The emergence and spread of Plasmodium falciparum human malaria parasites resistant to antimalarial drugs, including artemisinin, a first line antimalarial drug, is threatening malaria treatment and prompting fears of a resurgence of the disease. New drugs with novel mode of actions are thus urgently required. Several compounds with antimalarial activity are known to target protein translation, although few of these targets have been validated. Translation initiation in eukaryotes is known to require eukaryotic translation initiation factor 4F (eIF4F) complex, which binds to the 5′-cap structure on mature mRNA and recruits other proteins for translation of mRNA. The putative components of the eIF4F complex in P. falciparum have been identified in the genome including PfeIF4E, a 5′-cap-binding protein; PfeIF4A, a helicase protein for unwinding mRNA, and PfeIF4G, a PfeIF4E/PfeIF4A scaffold protein, which could constitute a novel antimalarial target. However, it is not known if these proteins constitute a P. falciparum eIF4F complex in vivo, nor what other proteins interact with the mRNA 5′-cap to control translation initiation in this species. Here, we investigated P. falciparum proteins that interact with the mRNA 5′-cap. Native protein extract from P. falciparum parasites was applied to m7GTP agarose beads and specific binding proteins eluted using m7GTP. LC-MS/MS based proteomic analysis of the m7GTP-eluted proteins demonstrated the presence of PfeIF4E, which was not found in control experiments with non-methylated GTP beads, verifying the native cap-binding function of PfeIF4E. PfeIF4A, PfeIF4G, and a putative polyadenylate-binding protein-interacting protein were present among m7GTP-eluted proteins but in low abundances. Interestingly, proteomics data clearly demonstrated P. falciparum enolase (Pfeno) in the m7GTP-eluted proteins.
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Project description:The emergence and spread of Plasmodium falciparum human malaria parasites resistant to antimalarial drugs, including artemisinin, a first line antimalarial drug, is threatening malaria treatment and prompting fears of a resurgence of the disease. New drugs with novel mode of actions are thus urgently required. Several compounds with antimalarial activity are known to target protein translation, although few of these targets have been validated. Translation initiation in eukaryotes is known to require eukaryotic translation initiation factor 4F (eIF4F) complex, which binds to the 5′-cap structure on mature mRNA and recruits other proteins for translation of mRNA. The putative components of the eIF4F complex in P. falciparum have been identified in the genome including PfeIF4E, a 5′-cap-binding protein; PfeIF4A, a helicase protein for unwinding mRNA, and PfeIF4G, a PfeIF4E/PfeIF4A scaffold protein, which could constitute a novel antimalarial target. However, it is not known if these proteins constitute a P. falciparum eIF4F complex in vivo, nor what other proteins interact with the mRNA 5′-cap to control translation initiation in this species. Here, we investigated P. falciparum proteins that interact with the mRNA 5′-cap. Native protein extract from P. falciparum parasites was applied to m7GTP agarose beads and specific binding proteins eluted using m7GTP. LC-MS/MS based proteomic analysis of the m7GTP-eluted proteins demonstrated the presence of PfeIF4E, which was not found in control experiments with non-methylated GTP beads, verifying the native cap-binding function of PfeIF4E. PfeIF4A, PfeIF4G, and a putative polyadenylate-binding protein-interacting protein were present among m7GTP-eluted proteins but in low abundances. Interestingly, proteomics data clearly demonstrated P. falciparum enolase (Pfeno) in the m7GTP-eluted proteins.
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Project description:Kynureninase is a member of a large family of catalytically diverse but structurally homologous pyridoxal 5'-phosphate (PLP) dependent enzymes known as the aspartate aminotransferase superfamily or alpha-family. The Homo sapiens and other eukaryotic constitutive kynureninases preferentially catalyze the hydrolytic cleavage of 3-hydroxy-l-kynurenine to produce 3-hydroxyanthranilate and l-alanine, while l-kynurenine is the substrate of many prokaryotic inducible kynureninases. The human enzyme was cloned with an N-terminal hexahistidine tag, expressed, and purified from a bacterial expression system using Ni metal ion affinity chromatography. Kinetic characterization of the recombinant enzyme reveals classic Michaelis-Menten behavior, with a Km of 28.3 +/- 1.9 microM and a specific activity of 1.75 micromol min-1 mg-1 for 3-hydroxy-dl-kynurenine. Crystals of recombinant kynureninase that diffracted to 2.0 A were obtained, and the atomic structure of the PLP-bound holoenzyme was determined by molecular replacement using the Pseudomonas fluorescens kynureninase structure (PDB entry 1qz9) as the phasing model. A structural superposition with the P. fluorescens kynureninase revealed that these two structures resemble the "open" and "closed" conformations of aspartate aminotransferase. The comparison illustrates the dynamic nature of these proteins' small domains and reveals a role for Arg-434 similar to its role in other AAT alpha-family members. Docking of 3-hydroxy-l-kynurenine into the human kynureninase active site suggests that Asn-333 and His-102 are involved in substrate binding and molecular discrimination between inducible and constitutive kynureninase substrates.
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