Modulation of mRNA Stability Participates in Stationary-Phase-Specific Expression of Ribosome Modulation Factor

Author:

Aiso Toshiko1,Yoshida Hideji2,Wada Akira2,Ohki Reiko1

Affiliation:

1. Department of Molecular Biology, School of Health Sciences, Kyorin University, Hachioji, Tokyo

2. Department of Physics, Osaka Medical College, Takatsuki, Osaka, Japan

Abstract

ABSTRACT The expression of ribosome modulation factor (RMF) is induced during stationary phase in Escherichia coli . RMF participates in the dimerization of 70S ribosomes to form the 100S ribosome, which is the translationally inactive form of the ribosome. To elucidate the involvement of the control of mRNA stability in growth-phase-specific rmf expression, we investigated rmf mRNA stability in stationary-phase cells and cells inoculated into fresh medium. The rmf mRNA was found to have an extremely long half-life during stationary phase, whereas destabilization of this mRNA took place after the culture was inoculated into fresh medium. RMF and 100S ribosomes disappeared from cells 1 min after inoculation. In addition to control by ppGpp-dependent transcription, these results indicate that the modulation of rmf mRNA stability is also involved in the regulation of growth-phase-specific rmf expression. Unexpectedly, the postinoculation degradation of rmf mRNA was suppressed by the addition of rifampin, suggesting that de novo RNA synthesis is necessary for degradation. This degradation was also suppressed in both a poly(A) polymerase-deficient and an rne-131 mutant strain. We cloned and sequenced the 3′-proximal regions of rmf mRNAs and found that most of these 3′ ends terminated at the ρ-independent terminator with the addition of a one- to five-A oligo(A) tail in either stationary-phase or inoculated cells. No difference was observed in the length of the poly(A) tail between stationary-phase and inoculated cells. These results suggest that a certain postinoculation-specific regulatory factor participates in the destabilization of rmf mRNA and is dependent on polyadenylation.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

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