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. 1985 Oct;164(1):57–62. doi: 10.1128/jb.164.1.57-62.1985

Pyrimidine-specific cleavage by an endoribonuclease of Saccharomyces cerevisiae.

A Stevens
PMCID: PMC214210  PMID: 3900048

Abstract

An endoribonuclease with pyrimidine cleavage site specificity was isolated from Saccharomyces cerevisiae. The enzyme had a pH optimum of 6 to 7 and did not require a divalent cation. It was inhibited by 5 X 10(-5) M ethidium bromide, although it appeared to be single strand specific. The enzyme gave a limited cleavage of yeast mRNA and rRNA, yielding products that were terminated with pyrimidine nucleoside 2',3'-cyclic phosphate. The bonds between pyrimidine and A residues constituted more than 90% of the scission sites when the average product size was 50 nucleotides. Homopolyribonucleotides were cleaved poorly. Poly(A,U) was cleaved rapidly, and analysis of the products of poly(A,U) hydrolysis showed a very stringent cleavage of U-A bonds.

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Selected References

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