A multiple mutant of Escherichia coli lacking the exoribonucleases RNase II, RNase D, and RNase BN

A multiple mutant strain of Escherichia coli containing mutations affecting the exoribonucleases, RNase II, RNase D, and RNase BN, and also the endonuclease, RNase I, was constructed by P1-mediated transduction. Extracts of the mutant strain were lacking the aforementioned RNase activities. The mult...

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Bibliographic Details
Published in:The Journal of biological chemistry 1984-10, Vol.259 (19), p.11651-11653
Main Authors: ZANIEWSKI, R, PETKAITIS, E, DEUTSCHER, M. P
Format: Article
Language:English
Subjects:
Biological and medical sciences
Endoribonucleases - metabolism
Escherichia coli - enzymology
Escherichia coli - genetics
Escherichia coli - growth & development
Escherichia coli Proteins
Exoribonucleases - metabolism
Fundamental and applied biological sciences. Psychology
Molecular and cellular biology
Molecular genetics
Mutation
Ribonuclease III
RNA - biosynthesis
T-Phages - metabolism
Transcription. Transcription factor. Splicing. Rna processing
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Summary:A multiple mutant strain of Escherichia coli containing mutations affecting the exoribonucleases, RNase II, RNase D, and RNase BN, and also the endonuclease, RNase I, was constructed by P1-mediated transduction. Extracts of the mutant strain were lacking the aforementioned RNase activities. The multiple mutant displayed normal growth in both rich and minimal media at a variety of temperatures, recovered from starvation essentially as the wild-type parent, and could support the growth of a variety of bacteriophages. In addition, RNA synthesis was normal and no precursor RNA accumulation was observed. The properties of the mutant strain indicate that the three exoribonucleases are not essential for the viability of E. coli. The implications of these findings to our understanding of RNA processing and degradation are discussed.
ISSN:0021-9258
1083-351X
DOI:10.1016/s0021-9258(20)71254-8