Polynucleotide phosphorylase is required for the rapid degradation of the RNase E-processed rpsO mRNA of Escherichia coli devoid of its 3' hairpin.

Abstract:

:The monocistronic transcript of rpsO undergoes an endonucleolytic cleavage downstream of the coding sequence, which removes the hairpin of the transcription terminator and initiates the rapid degradation of the message. We demonstrate here that the two rne-dependent cleavages, on both sides of the transcription terminator, are catalysed by RNase E in vitro and that the RNase E-processed rpsO message is rapidly degraded by polynucleotide phosphorylase, while RNase II produces stable decay intermediates. Moreover, we show that RNase E cuts in vitro the coding sequence of the rpsO mRNA at several sites which are not detected in vivo.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Braun F,Hajnsdorf E,Régnier P

doi

10.1046/j.1365-2958.1996.440971.x

subject

Has Abstract

pub_date

1996-03-01 00:00:00

pages

997-1005

issue

5

eissn

0950-382X

issn

1365-2958

journal_volume

19

pub_type

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