Biological activities of ribosome-inactivating proteins

Abstract

After more than 50 years of research, studies on the structure and biological activities of ribosome-inactivating proteins (RIPs) continue to provide a field of great interest within the scientific community, both for the health risks they pose and their applications in medicine and biotechnology. This Special Issue of Toxins offers a sample of the main research topics when studying these proteins. RIPs are ribosomal RNA N-glycosylases (EC 3.2.2.22), mainly isolated from plants, some bacteria, and fungi, that specifically catalyze the hydrolysis of the second N-glycosidic bond of the GAGA tetraloop located in the sarcin-ricin loop (SRL) of the major ribosomal RNA. Because SRL is crucial for anchoring elongation factors in the ribosome, the removal of adenine causes the irreversible inactivation of ribosomes, leading to cell death. In addition, RIPs usually demonstrate other enzymatic activities, including,most relevantly, their adenine polynucleotide glycosylase (APG) activity on all nucleic acid types; that is, some RIPs can remove adenines from both ribosomal and non-ribosomal RNA and DNA [1]. [Texto extraído del artículo de Lucía Citores González].