The transfer RNA processing defect in Escherichia coli strains BN and CAN is not due to a mutation in RNAase D or RNAase II

Pranab Roy, Henryk Cudny, Murray P Deutscher

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Escherichia coli strains BN and CAN are unable to support the growth of bacteriophage T4 psu1+-amber double mutants. For strain BN, this phenotype has been attributed to a defect in 3′ processing of the precursor to psu1+ tRNASer. Since RNAase D and RNAase II are the only well-characterized 3′ exoribonucleases to be implicated in tRNA processing, the status of these activities and their genes in the mutant strains was investigated. Although extracts of strains BN and CAN were defective for hydrolysis of the artificial tRNA precursor, tRNA-C-U, these strains contained normal levels of RNAase D and RNAase II, and purified RNAase D or RNAase II could only partially complement the mutant extracts. Introduction of the wild-type RNAase D gene into strains BN and CAN did not correct the mutant phenotype. Likewise, strains defective in RNAase D and/or RNAase II plated T4psu1+-amber phage normally. These results indicate that the tRNA processing defect in strains BN and CAN is not due to a mutation in either RNAase U or RNAase II. The possibility that the mutation in these strains affects another exoribonuclease or a factor influencing the activity and specificity of RNAase D or RNAase II is discussed.

Original languageEnglish
Pages (from-to)179-187
Number of pages9
JournalJournal of Molecular Biology
Volume159
Issue number1
DOIs
StatePublished - Jul 25 1982
Externally publishedYes

Fingerprint

Transfer RNA
Amber
Escherichia coli
Mutation
Exoribonucleases
RNA, Transfer, Ser
Phenotype
Bacteriophage T4
RNA Precursors
Bacteriophages
Genes
Hydrolysis
Growth

ASJC Scopus subject areas

  • Virology

Cite this

The transfer RNA processing defect in Escherichia coli strains BN and CAN is not due to a mutation in RNAase D or RNAase II. / Roy, Pranab; Cudny, Henryk; Deutscher, Murray P.

In: Journal of Molecular Biology, Vol. 159, No. 1, 25.07.1982, p. 179-187.

Research output: Contribution to journalArticle

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