Human Tissues Exhibit Diverse Composition of Translation Machinery

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,...

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Bibliographic Details
Published in:International journal of molecular sciences 2023-05, Vol.24 (9), p.8361
Main Authors: Anisimova, Aleksandra S, Kolyupanova, Natalia M, Makarova, Nadezhda E, Egorov, Artyom A, Kulakovskiy, Ivan V, Dmitriev, Sergey E
Format: Article
Language:English
Subjects:
Abundance
Amino Acyl-tRNA Synthetases
Aminoacyl-tRNA synthetases
aminoacyl-tRNA synthetases ARSases
Analysis
Cell differentiation
Composition
Efficiency
Elongation
Gene expression
Genes
Genetic translation
Human tissues
Humans
organ-specific translation
Organs
Peptide Elongation Factor 1
Peptide Initiation Factors
Protein biosynthesis
Protein synthesis
Proteins
proteome
Proteomics
Sex chromosomes
Sexual dimorphism
transcriptional landscape
transcriptome
Transcriptomics
Transfer RNA
Translation elongation
translation factors
Translation initiation
Translation termination
tRNA
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Summary: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.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms24098361