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WHEAT RIBOSOME-INACTIVATING PROTEINS - SEED AND LEAF FORMS WITH DIFFERENT SPECIFICITIES AND COFACTOR REQUIREMENTS
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UNSPECIFIED (1995) WHEAT RIBOSOME-INACTIVATING PROTEINS - SEED AND LEAF FORMS WITH DIFFERENT SPECIFICITIES AND COFACTOR REQUIREMENTS. PLANTA, 197 (4). pp. 633-640. ISSN 0032-0935.
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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.
Item Type: | Journal Article | ||||
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Subjects: | S Agriculture > SB Plant culture | ||||
Journal or Publication Title: | PLANTA | ||||
Publisher: | SPRINGER VERLAG | ||||
ISSN: | 0032-0935 | ||||
Official Date: | November 1995 | ||||
Dates: |
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Volume: | 197 | ||||
Number: | 4 | ||||
Number of Pages: | 8 | ||||
Page Range: | pp. 633-640 | ||||
Publication Status: | Published |
Data sourced from Thomson Reuters' Web of Knowledge
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