<i>Plasmodium</i>, the <i>Apicomplexa</i> Outlier When It Comes to Protein Synthesis
<i>Plasmodium</i> is an obligate intracellular parasite that has numerous interactions with different hosts during its elaborate life cycle. This is also the case for the other parasites belonging to the same phylum <i>Apicomplexa</i>. In this study, we bioinformatically iden...
| Main Authors: | , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2023-12-01
|
| Series: | Biomolecules |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2218-273X/14/1/46 |
| _version_ | 1797344561363681280 |
|---|---|
| author | José R. Jaramillo Ponce Magali Frugier |
| author_facet | José R. Jaramillo Ponce Magali Frugier |
| author_sort | José R. Jaramillo Ponce |
| collection | DOAJ |
| description | <i>Plasmodium</i> is an obligate intracellular parasite that has numerous interactions with different hosts during its elaborate life cycle. This is also the case for the other parasites belonging to the same phylum <i>Apicomplexa</i>. In this study, we bioinformatically identified the components of the multi-synthetase complexes (MSCs) of several <i>Apicomplexa</i> parasites and modelled their assembly using AlphaFold2. It appears that none of these MSCs resemble the two MSCs that we have identified and characterized in <i>Plasmodium</i>. Indeed, tRip, the central protein involved in the association of the two <i>Plasmodium</i> MSCs is different from its homologues, suggesting also that the tRip-dependent import of exogenous tRNAs is not conserved in other apicomplexan parasites. Based on this observation, we searched for obvious differences that could explain the singularity of <i>Plasmodium</i> protein synthesis by comparing tRNA genes and amino acid usage in the different genomes. We noted a contradiction between the large number of asparagine residues used in <i>Plasmodium</i> proteomes and the single gene encoding the tRNA that inserts them into proteins. This observation remains true for all the <i>Plasmodia</i> strains studied, even those that do not contain long asparagine homorepeats. |
| first_indexed | 2024-03-08T11:04:30Z |
| format | Article |
| id | doaj.art-8a9b19ad0be44082b9be1f57bdef9aac |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-03-08T11:04:30Z |
| publishDate | 2023-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-8a9b19ad0be44082b9be1f57bdef9aac2024-01-26T15:18:40ZengMDPI AGBiomolecules2218-273X2023-12-011414610.3390/biom14010046<i>Plasmodium</i>, the <i>Apicomplexa</i> Outlier When It Comes to Protein SynthesisJosé R. Jaramillo Ponce0Magali Frugier1Université de Strasbourg, CNRS, Architecture et Réactivité de l’ARN, UPR 9002, F-67084 Strasbourg, FranceUniversité de Strasbourg, CNRS, Architecture et Réactivité de l’ARN, UPR 9002, F-67084 Strasbourg, France<i>Plasmodium</i> is an obligate intracellular parasite that has numerous interactions with different hosts during its elaborate life cycle. This is also the case for the other parasites belonging to the same phylum <i>Apicomplexa</i>. In this study, we bioinformatically identified the components of the multi-synthetase complexes (MSCs) of several <i>Apicomplexa</i> parasites and modelled their assembly using AlphaFold2. It appears that none of these MSCs resemble the two MSCs that we have identified and characterized in <i>Plasmodium</i>. Indeed, tRip, the central protein involved in the association of the two <i>Plasmodium</i> MSCs is different from its homologues, suggesting also that the tRip-dependent import of exogenous tRNAs is not conserved in other apicomplexan parasites. Based on this observation, we searched for obvious differences that could explain the singularity of <i>Plasmodium</i> protein synthesis by comparing tRNA genes and amino acid usage in the different genomes. We noted a contradiction between the large number of asparagine residues used in <i>Plasmodium</i> proteomes and the single gene encoding the tRNA that inserts them into proteins. This observation remains true for all the <i>Plasmodia</i> strains studied, even those that do not contain long asparagine homorepeats.https://www.mdpi.com/2218-273X/14/1/46tRNAamino acid usageAlphaFold2 modelingmulti-synthetase complexestranslational control |
| spellingShingle | José R. Jaramillo Ponce Magali Frugier <i>Plasmodium</i>, the <i>Apicomplexa</i> Outlier When It Comes to Protein Synthesis Biomolecules tRNA amino acid usage AlphaFold2 modeling multi-synthetase complexes translational control |
| title | <i>Plasmodium</i>, the <i>Apicomplexa</i> Outlier When It Comes to Protein Synthesis |
| title_full | <i>Plasmodium</i>, the <i>Apicomplexa</i> Outlier When It Comes to Protein Synthesis |
| title_fullStr | <i>Plasmodium</i>, the <i>Apicomplexa</i> Outlier When It Comes to Protein Synthesis |
| title_full_unstemmed | <i>Plasmodium</i>, the <i>Apicomplexa</i> Outlier When It Comes to Protein Synthesis |
| title_short | <i>Plasmodium</i>, the <i>Apicomplexa</i> Outlier When It Comes to Protein Synthesis |
| title_sort | i plasmodium i the i apicomplexa i outlier when it comes to protein synthesis |
| topic | tRNA amino acid usage AlphaFold2 modeling multi-synthetase complexes translational control |
| url | https://www.mdpi.com/2218-273X/14/1/46 |
| work_keys_str_mv | AT joserjaramilloponce iplasmodiumitheiapicomplexaioutlierwhenitcomestoproteinsynthesis AT magalifrugier iplasmodiumitheiapicomplexaioutlierwhenitcomestoproteinsynthesis |