Structures of eukaryotic ribosomal stalk proteins and its complex with trichosanthin, and their implications in recruiting ribosome-inactivating proteins to the ribosomes

Toxins (Basel). 2015 Feb 25;7(3):638-47. doi: 10.3390/toxins7030638.


Ribosome-inactivating proteins (RIP) are RNA N-glycosidases that inactivate ribosomes by specifically depurinating a conserved adenine residue at the α-sarcin/ricin loop of 28S rRNA. Recent studies have pointed to the involvement of the C-terminal domain of the eukaryotic stalk proteins in facilitating the toxic action of RIPs. This review highlights how structural studies of eukaryotic stalk proteins provide insights into the recruitment of RIPs to the ribosomes. Since the C-terminal domain of eukaryotic stalk proteins is involved in specific recognition of elongation factors and some eukaryote-specific RIPs (e.g., trichosanthin and ricin), we postulate that these RIPs may have evolved to hijack the translation-factor-recruiting function of ribosomal stalk in reaching their target site of rRNA.

Publication types

  • Review

MeSH terms

  • Archaeal Proteins / chemistry
  • Archaeal Proteins / genetics
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Eukaryota / chemistry
  • Eukaryota / genetics
  • Models, Molecular
  • Protein Conformation
  • Ribosome Inactivating Proteins / chemistry*
  • Ribosome Inactivating Proteins / genetics
  • Ribosomes / chemistry*
  • Ricin / chemistry
  • Trichosanthin / chemistry*


  • Archaeal Proteins
  • Bacterial Proteins
  • Trichosanthin
  • Ricin
  • Ribosome Inactivating Proteins