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Papers In Press, published online ahead of print February 10, 2003
Division of Biological Science, Nagoya University, Nagoya, Aichi 464-8602
Corresponding Author: i45346a{at}nucc.cc.nagoya-u.ac.jp
Previously, we found that a mutation in either the pgi or pfkA, encoding phosphoglucose isomerase or phosphofructokinase A, facilitates degradation of the ptsG mRNA in an RNase E-dependent manner in Escherichia coli (1). In this paper, 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-diphosphate aldolase just downstream of pfkA in the glycolytic pathway, caused the destabilization of ptsG mRNA at the nonpermissive temperature. Mutations in any other genes did not destabilize the ptsG mRNA while they reduced the ptsG transcription mainly by affecting cAMP level. The rapid degradation of ptsG mRNA in mutant strains was completely dependent upon the presence of glucose or any one of 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-phosphate also led to the rapid degradation of ptsG mRNA in a pgi pfkA mutant strain lacking glucose-6-phosphate. We conclude that the RNase E-dependent destabilization of ptsG mRNA occurs in response to accumulation of glucose-6-phosphate or fructose-6-phosphate.
J. Biol. Chem, 10.1074/jbc.M300177200
Submitted on January 8, 2003
Revised on February 10, 2003
Accepted on February 10, 2003
Accumulation of glucose-6-phosphate or fructose-6-phosphate is responsible for destabilization of glucose transporter mRNA in Escherichia coli
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