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Musarmins: Three single-chain ribosome-inactivating protein isoforms from bulbs of Muscari armeniacum L. and Miller

TitleMusarmins: Three single-chain ribosome-inactivating protein isoforms from bulbs of Muscari armeniacum L. and Miller
Publication TypeArticolo su Rivista peer-reviewed
Year of Publication2003
AuthorsArias, F.J., Antolín P., De Torre C., Barriuso B., Iglesias R., Rojo M.A., Ferreras J.M., Benvenuto Eugenio, Méndez E., and Girbés T.
JournalInternational Journal of Biochemistry and Cell Biology
Pagination61 - 78
Date Published2003
ISBN Number13572725 (ISSN)
KeywordsAmino Acid, amino acid derivative, Amino Acid Sequence, angiosperm, animal, Animals, article, Base Sequence, carboxy terminal sequence, chemistry, Cloning, complementary DNA, concentration response, controlled study, darkness, drug effect, Electrophoresis, gel filtration, gene expression regulation, genetics, glycosidase, HeLa cell, human, human cell, Hydrogen Peroxide, IC 50, Inhibitors, Inhibitory Concentration 50, intron, ion exchange chromatography, isoprotein, life cycle, Liliaceae, Mass Spectrometry, messenger RNA, metabolism, Molecular, molecular cloning, molecular genetics, Molecular Sequence Data, musarmin, Musarmins, Muscari armeniacum, N-Glycosidase, N-Glycosyl Hydrolases, nucleotide sequence, open reading frame, Plant, plant bulb, plant cell, plant growth, plant leaf, Plant Proteins, plant tuber, Plant Tubers, protein analysis, Protein Isoforms, protein isolation, protein processing, protein synthesis inhibition, protein synthesis inhibitor, Protein Synthesis Inhibitors, rabbit, Rabbits, reticulocyte, Reticulocytes, ribosome, ribosome inactivating protein, Ribosome-inactivating protein, Ribosomes, RNA 28S, rRNA, salicylic acid, senescence, sequence homology, Translation, unclassified drug, untranslated RNA, vegetable protein

Three new ribosome-inactivating protein (RIP; EC isoforms that we have named musarmins (MUs) 1, 2 and 3 have been isolated from the bulbs of Muscari armeniacum L. and Miller by ion-exchange chromatography and gel filtration. Analysis by electrophoresis revealed that they are single-chain proteins and mass spectrometry analysis afforded Mr values of 28,708,30,003 and 27,626 for MUs 1, 2 and 3, respectively. Musarmins strongly inhibited protein synthesis carried out by mammalian ribosomes, with IC50 values in the 0.14-0.24nM range but not that carried out by plant cell-free systems or HeLa cells. MUs promote the single depurination of rabbit reticulocyte 28S rRNA. cDNA cloning of genes coding for musarmins revealed that they contain open reading frames of 298, 294 and 295 aminoacids for MU1, MU2 and MU3, respectively. Mature MU1, MU2 and MU3 contain 277, 273 and 273 aminoacids, respectively suggesting post-translational C-terminal processing. An untranslated mRNA coding for an ORF very similar to that of MU3 was detected in leaves. Each of the four MU genes contains an intron. In contrast to other RIPs, MUs are present only in bulbs and are not induced in leaves either by senescence, or by treatment of leaves with H2O2 or salicylic acid, or by growth in darkness. Therefore, these proteins could play a non-vital role in plants; for instance, as anti-pathogens and protective agents only in some stages of the plant life cycle (237). © 2002 Elsevier Science Ltd. All rights reserved.


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