Structures and Ribosomal Interaction of Ribosome-Inactivating Proteins

Molecules. 2016 Nov 21;21(11):1588. doi: 10.3390/molecules21111588.

Abstract

Ribosome-inactivating proteins (RIPs) including ricin, Shiga toxin, and trichosanthin, are RNA N-glycosidases that depurinate a specific adenine residue (A-4324 in rat 28S ribosomal RNA, rRNA) in the conserved α-sarcin/ricin loop (α-SRL) of rRNA. RIPs are grouped into three types according to the number of subunits and the organization of the precursor sequences. RIPs are two-domain proteins, with the active site located in the cleft between the N- and C-terminal domains. It has been found that the basic surface residues of the RIPs promote rapid and specific targeting to the ribosome and a number of RIPs have been shown to interact with the C-terminal regions of the P proteins of the ribosome. At present, the structural basis for the interaction of trichosanthin and ricin-A chain toward P2 peptide is known. This review surveys the structural features of the representative RIPs and discusses how they approach and interact with the ribosome.

Keywords: P proteins; RNA N-glycosidases; ribosomal interaction; ribosome; ribosome-inactivating proteins.

Publication types

  • Review

MeSH terms

  • Catalytic Domain
  • Models, Molecular*
  • Molecular Structure*
  • Protein Binding
  • Protein Interaction Domains and Motifs
  • Ribosome Inactivating Proteins / chemistry*
  • Ribosome Inactivating Proteins / classification
  • Ribosome Inactivating Proteins / metabolism
  • Ribosome Subunits / genetics
  • Ribosome Subunits / metabolism
  • Ribosomes / chemistry*
  • Structure-Activity Relationship
  • Substrate Specificity

Substances

  • Ribosome Inactivating Proteins