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Peculiarities of aminoacyl-tRNA synthetases from trypanosomatids
- Source :
- Journal of Biological Chemistry, Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2021, 297 (2), pp.100913. ⟨10.1016/j.jbc.2021.100913⟩, The Journal of Biological Chemistry
- Publication Year :
- 2021
- Publisher :
- HAL CCSD, 2021.
-
Abstract
- Trypanosomatid parasites are responsible for various human diseases, such as sleeping sickness, animal trypanosomiasis, or cutaneous and visceral leishmaniases. The few available drugs to fight related parasitic infections are often toxic and present poor efficiency and specificity, and thus, finding new molecular targets is imperative. Aminoacyl-tRNA synthetases (aaRSs) are essential components of the translational machinery as they catalyze the specific attachment of an amino acid onto cognate tRNA(s). In trypanosomatids, one gene encodes both cytosolic- and mitochondrial-targeted aaRSs, with only three exceptions. We identify here a unique specific feature of aaRSs from trypanosomatids, which is that most of them harbor distinct insertion and/or extension sequences. Among the 26 identified aaRSs in the trypanosome Leishmania tarentolae, 14 contain an additional domain or a terminal extension, confirmed in mature mRNAs by direct cDNA nanopore sequencing. Moreover, these RNA-Seq data led us to address the question of aaRS dual localization and to determine splice-site locations and the 5'-UTR lengths for each mature aaRS-encoding mRNA. Altogether, our results provided evidence for at least one specific mechanism responsible for mitochondrial addressing of some L. tarentolae aaRSs. We propose that these newly identified features of trypanosomatid aaRSs could be developed as relevant drug targets to combat the diseases caused by these parasites.
- Subjects :
- 0301 basic medicine
[SDV]Life Sciences [q-bio]
Trans-splicing
MTS, mt targeting sequence
Computational biology
Biology
Biochemistry
Amino Acyl-tRNA Synthetases
03 medical and health sciences
chemistry.chemical_compound
Cytosol
RNA, Transfer
aaRSs, aminoacyl-tRNA synthetases
Complementary DNA
Animals
Humans
aminoacyl-tRNA synthetase
MARS, multi-aaRS complex
NTD, N-terminal domain
Amino Acid Sequence
Amino Acids
Leishmaniasis
Molecular Biology
Gene
Phylogeny
ComputingMilieux_MISCELLANEOUS
Leishmania
chemistry.chemical_classification
trans-splicing
Multiple sequence alignment
Sequence Homology, Amino Acid
030102 biochemistry & molecular biology
Aminoacyl tRNA synthetase
C-terminus
Cell Biology
species-specific insertions/extensions
CTD, C-terminal domain
Mitochondria
3. Good health
Amino acid
kinetoplastids
MSA, multiple sequence alignment
030104 developmental biology
chemistry
Transfer RNA
mt, mitochondrial
Research Article
Subjects
Details
- Language :
- English
- ISSN :
- 00219258 and 1083351X
- Database :
- OpenAIRE
- Journal :
- Journal of Biological Chemistry, Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2021, 297 (2), pp.100913. ⟨10.1016/j.jbc.2021.100913⟩, The Journal of Biological Chemistry
- Accession number :
- edsair.doi.dedup.....dacf02e49230ad2b20b5f2b86b5dbdfc