Hydroxylation of protein constituents of the human translation system: Structural aspects and functional assignments

Dmitri Graifer, Alexey Malygin, Galina Karpova

Research output: Contribution to journalReview articlepeer-review

1 Citation (Scopus)

Abstract

During the current decade, data on the post-translational hydroxylation of specific amino acid residues of some ribosomal proteins and translation factors in both eukaryotes and eubacteria have accumulated. The reaction is catalyzed by dedicated oxygenases (so-called ribosomal oxygenases), whose action is impaired under hypoxia conditions. The modification occurs at amino acid residues directly involved in the formation of the main functional sites of ribosomes and factors. This review summarizes currently available data on the specific hydroxylation of protein constituents of eukaryotic and eubacterial translation systems with a special emphasis on the human system, as well as on the links between hypoxia impacts on the operation of ribosomal oxygenases, the functioning of the translational apparatus and human health problems.

Original languageEnglish
Pages (from-to)357-369
Number of pages13
JournalFuture Medicinal Chemistry
Volume11
Issue number4
DOIs
Publication statusPublished - 1 Feb 2019

Keywords

  • health disorders
  • hypoxia
  • ribosomal proteins
  • ribosome oxygenases
  • specific hydroxylation of proteins
  • translation factors
  • translation regulation dysfunctions

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