Wheat ribosome-inactivating proteins: Seed and leaf forms with different specificities and cofactor requirements |
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Authors: | Andrea J Massiah Martin R Hartley |
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Institution: | (1) Department of Biological Sciences, University of Warwick, CV4 7AL Coventry, West Midlands, UK |
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Abstract: | Distinct forms of ribosome-inactivating proteins were purified from wheat (Triticum aestivum L.) germ and leaves and termed tritin-S and tritin-L, respectively. These differ in size and charge and are antigenically unrelated. They are both RNA N-glycosidases which act on 26S rRNA in native yeast (Saccharomyces cerevisiae) ribosomes by the removal of A3024 located in a universally conserved sequence in domain VII which has previously been identified as the site of action of ricin A-chain. Tritin-S and tritin-L differ in both their ribosome substrate specificities and cofactor requirements. Tritin-S shows only barely detectable activity on ribosomes from the endosperm, its tissue of synthesis, whereas tritin-L is highly active on leaf ribosomes. Additionally, tritin-S is inactive on wheat germ, tobacco leaf and Escherichia coli ribosomes but active on rabbit reticulocyte and yeast ribosomes. Tritin-L is active on ribosomes from all of the above sources. Tritin-S, unlike tritin-L shows a marked requirement for ATP in its action.Abbreviations CM
carboxymethyl
- FPLC
fast protein liquid chromatography
- NEPHGE
non-equilibrium pH gradient gel electrophoresis
- PAP
pokeweed antiviral protein
- RIP
ribosome-inactivating protein
A.J.M. was the recipient of a U.K. Science and Engineering Research Council CASE studentship sponsored by Agricultural Genetics Company Ltd., Cambridge CB4 4GG, UK. |
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Keywords: | Ribosome inactivating protein (isoenzymes specificity) RNA N-glycosidase Triticum |
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