α-Sarcin cleaves ribosomal RNA at the α-sarcin site in the absence of ribosomal proteins

Stephen P Miller; James W. Bodley

doi:10.1016/0006-291X(88)90700-0

α-Sarcin cleaves ribosomal RNA at the α-sarcin site in the absence of ribosomal proteins

Stephen P Miller, James W. Bodley

Biotechnology Institute

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

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Abstract

α-Sarcin is capable of specifically cleaving the single phosphodiester bond in the "α-sarcin site" of both Escherichia coli and Saccharomyces cerevisiae large rRNAs in the absence of ribosomal proteins. With both sources of rRNA, the rate of cleavage was comparable with and without ribosomal proteins but more complete cleavage was observed in the absence of ribosomal proteins. These observations contrast with earlier findings and indicate that ribosomal proteins are not essential to the unique specificity of the cleavage of rRNA by α-sarcin.

Original language	English (US)
Pages (from-to)	404-410
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	154
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(88)90700-0
State	Published - Jul 15 1988

Bibliographical note

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

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AU - Bodley, James W.

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AB - α-Sarcin is capable of specifically cleaving the single phosphodiester bond in the "α-sarcin site" of both Escherichia coli and Saccharomyces cerevisiae large rRNAs in the absence of ribosomal proteins. With both sources of rRNA, the rate of cleavage was comparable with and without ribosomal proteins but more complete cleavage was observed in the absence of ribosomal proteins. These observations contrast with earlier findings and indicate that ribosomal proteins are not essential to the unique specificity of the cleavage of rRNA by α-sarcin.

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α-Sarcin cleaves ribosomal RNA at the α-sarcin site in the absence of ribosomal proteins

Abstract

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