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. 1983 Jun;80(11):3301–3304. doi: 10.1073/pnas.80.11.3301

Ribonuclease BN: identification and partial characterization of a new tRNA processing enzyme.

P K Asha, R T Blouin, R Zaniewski, M P Deutscher
PMCID: PMC394029  PMID: 6344080

Abstract

A new ribonuclease, RNase BN, has been identified and partially purified from a strain of Escherichia coli lacking RNase II and RNase D by using the artificial tRNA precursor tRNA-C-[14C]U as substrate. This enzyme is present in E. coli B but absent from the tRNA processing mutant strain BN which is unable to process extraneous 3' residues on certain phage T4-specified tRNA precursors. The properties of RNase BN clearly distinguish this enzyme from other known E. coli exoribonucleases. It is optimally active at pH 6.5 with 0.2 mM divalent cation and 0.2 M monovalent cation. It is most active against tRNA substrates containing nucleotide substitutions within the -C-C-A sequence and relatively inactive against other types of RNAs. This substrate specificity in vitro is consistent with a processing function in vivo. However, in contrast to the other processing enzymes whose function has been confirmed by mutation, RNase BN is an exoribonuclease. The presence of multiple RNases in E. coli and a strategy for their identification and separation are discussed.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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