bioRxiv Science⌕ Search

Biology subjects

Jaramillo Ponce, J. R.

Publications and source records attributed to Jaramillo Ponce, J. R..

2 recordsLinked to original sources

RlmQ: A Newly Discovered rRNA Modification Enzyme Bridging RNA Modification and Virulence Traits in Staphylococcus aureus

rRNA modifications play crucial roles in fine-tuning the delicate balance between translation speed and accuracy, yet the underlying mechanisms remain elusive. Comparative analysis of the ribosomal RNA modifications in taxonomically distant bacteria could help define their general as well as species-specific roles. In this study, we identified a new methyltransferase, RlmQ, in Staphylococcus aureus responsible for the Gram-positive specific m7G2601, which is not modified in E. coli (G2574). We also demonstrate the absence of methylation on C1989, equivalent to E. coli C1962, which is methylated at position 5 by the Gram-negative specific RlmI methyltransferase, a paralogue of RlmQ. Both modifications (S. aureus m7G2601 and E. coli m5C1962) are situated within the same tRNA accommodation corridor, hinting at a potential shared function in translation. Inactivation of S. aureus rlmQ causes the loss of methylation at G2601 and significantly impacts growth, cytotoxicity, and biofilm formation. These findings unravel the intricate connections between rRNA modifications, translation, and virulence in pathogenic Gram-positive bacteria.

molecular biology↗

Plasmodium, the Apicomplexa outlier when it comes to protein synthesis

Plasmodium is an obligate intracellular parasite that makes numerous interactions with different hosts during its elaborate life cycle. This is also the case for other parasites that belong to the same phylum Apicomplexa. In this study, we identified bioinformatically the components of the multi-synthetase complexes (MSC) of several Apicomplexa parasites. By using AlphaFold2 modeling to compare their assembly, it appears that none of these MSCs resemble those identified in Plasmodium. In particular, the discrepancies between the core components of Plasmodium complexes, tRip and its homologs indicate that tRip-dependent exogenous tRNA import is not conserved in the other Apicomplexa parasites. Based on this observation, we looked for obvious differences that could explain this singularity in Plasmodium. The content of tRNA genes and amino acid usage in the different genomes highlighted the originality of Plasmodia translation. This is evident with respect to asparagine amino acid, which is highly used in the Plasmodium proteomes, and the scarcity of tRNAAsn required for protein synthesis, regardless of long homorepeats or AT content of the genomes.

microbiology↗