Human Tissues Exhibit Diverse Composition of Translation Machinery

Int J Mol Sci. 2023 May 6;24(9):8361. doi: 10.3390/ijms24098361.

Abstract

While protein synthesis is vital for the majority of cell types of the human body, diversely differentiated cells require specific translation regulation. This suggests the specialization of translation machinery across tissues and organs. Using transcriptomic data from GTEx, FANTOM, and Gene Atlas, we systematically explored the abundance of transcripts encoding translation factors and aminoacyl-tRNA synthetases (ARSases) in human tissues. We revised a few known and identified several novel translation-related genes exhibiting strict tissue-specific expression. The proteins they encode include eEF1A1, eEF1A2, PABPC1L, PABPC3, eIF1B, eIF4E1B, eIF4ENIF1, and eIF5AL1. Furthermore, our analysis revealed a pervasive tissue-specific relative abundance of translation machinery components (e.g., PABP and eRF3 paralogs, eIF2B and eIF3 subunits, eIF5MPs, and some ARSases), suggesting presumptive variance in the composition of translation initiation, elongation, and termination complexes. These conclusions were largely confirmed by the analysis of proteomic data. Finally, we paid attention to sexual dimorphism in the repertoire of translation factors encoded in sex chromosomes (eIF1A, eIF2γ, and DDX3), and identified the testis and brain as organs with the most diverged expression of translation-associated genes.

Keywords: aminoacyl-tRNA synthetases ARSases; cell type-specific translation; gonads; neurons; organ-specific translation; proteome; sexual dimorphism; transcriptional landscape; transcriptome; translation factors.

MeSH terms

  • Amino Acyl-tRNA Synthetases*
  • Humans
  • Peptide Elongation Factor 1
  • Peptide Initiation Factors
  • Proteomics*

Substances

  • Amino Acyl-tRNA Synthetases
  • Peptide Initiation Factors
  • EEF1A2 protein, human
  • Peptide Elongation Factor 1