Modification of ribosomal RNA by ribosome-inactivating proteins from plants

Fiorenzo Stirpe; Suzanne Bailey; Stephen P. Miller; James W. Bodley

doi:10.1093/nar/16.4.1349

Modification of ribosomal RNA by ribosome-inactivating proteins from plants

Fiorenzo Stirpe, Suzanne Bailey, Stephen P. Miller, James W. Bodley

Biotechnology Institute

Research output: Contribution to journal › Article › peer-review

137 Scopus citations

Abstract

We have survayed 14 different toxic and nontoxic ribosome-inactivating proteins from plants for the ability to act on the RNA of the eucaryotic 60 S ribosomal subunit. All of these proteins act to introduce a specific modification into 26-28 S RNA which renders the RNA sensitive to cleavage by aniline. Sequence analysis of the 5′-termini of the fragments produced by ricin and saporin following aniline cleavage indicate that both proteins possess identical specificity. Our obaervations support the conclusion of Endo and Tsurugi (J. Biol. Chem. 262, 8128-8130, 1987) that ricin is a specific N-glycoaidase and we have located the site of this cleavage by direct sequence analysis. Our results further suggest that all plant ribosome-inactivating proteins function as specific N-glycosidases with tha same specificity.

Original language	English (US)
Pages (from-to)	1349-1357
Number of pages	9
Journal	Nucleic acids research
Volume	16
Issue number	4
DOIs	https://doi.org/10.1093/nar/16.4.1349
State	Published - Feb 25 1988

Bibliographical note

Funding Information:
ACKNOWLEDGMENTS: This work was supported by grants from the NIH (GM-26832), the Graduate School of the University of Minnesota and the Minnesota Medical Foundation.

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abstract = "We have survayed 14 different toxic and nontoxic ribosome-inactivating proteins from plants for the ability to act on the RNA of the eucaryotic 60 S ribosomal subunit. All of these proteins act to introduce a specific modification into 26-28 S RNA which renders the RNA sensitive to cleavage by aniline. Sequence analysis of the 5′-termini of the fragments produced by ricin and saporin following aniline cleavage indicate that both proteins possess identical specificity. Our obaervations support the conclusion of Endo and Tsurugi (J. Biol. Chem. 262, 8128-8130, 1987) that ricin is a specific N-glycoaidase and we have located the site of this cleavage by direct sequence analysis. Our results further suggest that all plant ribosome-inactivating proteins function as specific N-glycosidases with tha same specificity.",

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AU - Bailey, Suzanne

AU - Miller, Stephen P.

AU - Bodley, James W.

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AB - We have survayed 14 different toxic and nontoxic ribosome-inactivating proteins from plants for the ability to act on the RNA of the eucaryotic 60 S ribosomal subunit. All of these proteins act to introduce a specific modification into 26-28 S RNA which renders the RNA sensitive to cleavage by aniline. Sequence analysis of the 5′-termini of the fragments produced by ricin and saporin following aniline cleavage indicate that both proteins possess identical specificity. Our obaervations support the conclusion of Endo and Tsurugi (J. Biol. Chem. 262, 8128-8130, 1987) that ricin is a specific N-glycoaidase and we have located the site of this cleavage by direct sequence analysis. Our results further suggest that all plant ribosome-inactivating proteins function as specific N-glycosidases with tha same specificity.

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Modification of ribosomal RNA by ribosome-inactivating proteins from plants

Abstract

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