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Toxins 2015, 7(3), 638-647; doi:10.3390/toxins7030638

Structures of Eukaryotic Ribosomal Stalk Proteins and Its Complex with Trichosanthin, and Their Implications in Recruiting Ribosome-Inactivating Proteins to the Ribosomes

School of Life Sciences, the Chinese University of Hong Kong, Shatin, Hong Kong, China
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Academic Editor: Nilgun E. Tumer
Received: 28 November 2014 / Revised: 30 January 2015 / Accepted: 15 February 2015 / Published: 25 February 2015
(This article belongs to the Special Issue Plant Toxins)
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Abstract

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. View Full-Text
Keywords: ribosome; trichosanthin; ricin; stalk; ribosome inactivating proteins; elongation factors ribosome; trichosanthin; ricin; stalk; ribosome inactivating proteins; elongation factors
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Choi, A.K.H.; Wong, E.C.K.; Lee, K.-M.; Wong, K.-B. Structures of Eukaryotic Ribosomal Stalk Proteins and Its Complex with Trichosanthin, and Their Implications in Recruiting Ribosome-Inactivating Proteins to the Ribosomes. Toxins 2015, 7, 638-647.

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