RIBOSOME-INACTIVATINGPROTEINS: A Plant Perspective
- 1 June 2001
- journal article
- review article
- Published by Annual Reviews in Annual Review of Plant Biology
- Vol. 52 (1) , 785-816
- https://doi.org/10.1146/annurev.arplant.52.1.785
Abstract
▪ Abstract Ribosome-inactivating proteins (RIPs) are toxic N-glycosidases that depurinate the universally conserved α-sarcin loop of large rRNAs. This depurination inactivates the ribosome, thereby blocking its further participation in protein synthesis. RIPs are widely distributed among different plant genera and within a variety of different tissues. Recent work has shown that enzymatic activity of at least some RIPs is not limited to site-specific action on the large rRNAs of ribosomes but extends to depurination and even nucleic acid scission of other targets. Characterization of the physiological effects of RIPs on mammalian cells has implicated apoptotic pathways. For plants, RIPs have been linked to defense by antiviral, antifungal, and insecticidal properties demonstrated in vitro and in transgenic plants. How these effects are brought about, however, remains unresolved. At the least, these results, together with others summarized here, point to a complex biological role. With genetic, genomic, mo...This publication has 213 references indexed in Scilit:
- Trichosanthin Interacts with and Enters Cells via LDL Receptor Family MembersBiochemical and Biophysical Research Communications, 2000
- Site-Specific Mutagenesis of Mistletoe Lectin: The Role of RIP Activity in ApoptosisBiochemical and Biophysical Research Communications, 1999
- Proteolytic Fragments of Anti-HIV and Anti-tumor Proteins MAP30 and GAP31 Are Biologically ActiveBiochemical and Biophysical Research Communications, 1999
- Pokeweed Antiviral Protein Isoforms PAP-I, PAP-II, and PAP-III Depurinate RNA of Human Immunodeficiency Virus (HIV)-1Biochemical and Biophysical Research Communications, 1999
- Differences in Cytotoxicity of Native and Engineered RIPs Can Be Used to Assess Their Ability to Reach the CytoplasmBiochemical and Biophysical Research Communications, 1998
- Position 120–123, a potential active site of trichosanthinLife Sciences, 1998
- Demonstration of ribonuclease activity in the plant ribosome-inactivating proteins alpha- and beta- momorcharinsLife Sciences, 1996
- Ribosome-inactivating proteins from plantsBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1993
- High sensitivity of cultured human trophoblasts to ribosome-inactivating proteinsExperimental Cell Research, 1992
- Ribosomal RNA identity elements for ricin A-chain recognition and catalysisJournal of Molecular Biology, 1991