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
Subjects:	S Agriculture > SB Plant culture
Journal or Publication Title:	PLANTA
Publisher:	SPRINGER VERLAG
ISSN:	0032-0935
Date:	November 1995
Volume:	197
Number:	4
Number of Pages:	8
Page Range:	pp. 633-640
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/19228

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