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J. Biol. Chem., Vol. 278, Issue 18, 15608-15614, May 2, 2003
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From the Division of Biological Science, Graduate School of
Science, Nagoya University, Chikusa, Nagoya 464-8602, Japan
Previously we found that a mutation in
either pgi or pfkA, encoding phosphoglucose
isomerase or phosphofructokinase A, respectively, facilitates
degradation of the ptsG mRNA in an RNase
E-dependent manner in Escherichia coli (1). In
this study, we examined the effects of a series of glycolytic genes on
the degradation of ptsG mRNA and how the mutations
destabilize the ptsG mRNA. The conditional lethal
mutation ts8 in fda, encoding
fructose-1,6-P2 aldolase just downstream of
pfkA in the glycolytic pathway, caused the destabilization
of ptsG mRNA at the nonpermissive temperature. Mutations in any other gene did not destabilize the ptsG
mRNA; rather, they reduced the ptsG transcription
mainly by affecting the cAMP level. The rapid degradation of
ptsG mRNA in mutant strains was completely dependent
upon the presence of glucose or any one of its compounds, which enter
the Embden-Meyerhof glycolytic pathway before the block points. A
significant increase in the intracellular glucose-6-P level was
observed in the presence of glucose in the pgi strain. An
overexpression of glucose-6-phosphate dehydrogenase eliminated
both the accumulation and the degradation of ptsG mRNA in the pgi strain. In addition, accumulation of
fructose-6-P led to the rapid degradation of ptsG mRNA
in a pgi pfkA mutant strain lacking glucose-6-P. We
conclude that the RNase E-dependent destabilization of
ptsG mRNA occurs in response to accumulation of
glucose-6-P or fructose-6-P.
To whom correspondence should be addressed. Tel.: 81-52-789-3653;
Fax: 81-52-789-3001; E-mail: i45346a@nucc.cc.nagoya-u.ac.jp.
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