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Journal of Bacteriology, August 2001, p. 4493-4498, Vol. 183, No. 15
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.15.4493-4498.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Properties of a Revertant of Escherichia coli Viable in the Presence of Spermidine Accumulation: Increase in L-Glycerol 3-Phosphate

V. Samuel Raj,1 Hideyuki Tomitori,1 Madoka Yoshida,1 Auayporn Apirakaramwong,1 Keiko Kashiwagi,1 Koji Takio,2 Akira Ishihama,3 and Kazuei Igarashi1,*

Graduate School of Pharmaceutical Sciences, Chiba University, Inage-ku, Chiba 263-8522,1 Division of Biomolecular Characterization, Institute of Physical and Chemical Research (RIKEN), 2-1 Hirosawa, Wako-shi, Saitama 350-0106,2 and Department of Molecular Genetics, National Institute of Genetics, Mishima, Shizuoka 411-0801,3 Japan

Received 12 February 2001/Accepted 11 May 2001

Escherichia coli CAG2242 cells are deficient in the speG gene encoding spermidine acetyltransferase. When these cells were cultured in the presence of 0.5 to 4 mM spermidine, their viability was greatly decreased through the inhibition of protein synthesis by overaccumulation of spermidine. When the cells were cultured with a high concentration of spermidine (4 mM), a revertant strain was obtained. We found that a 55-kDa protein, glycerol kinase, was overexpressed in the revertant and that synthesis of a ribosome modulation factor and the RNA polymerase sigma 38 subunit, factors important for cell viability, was increased in the revertant. Levels of L-glycerol 3-phosphate also increased in the revertant. Transformation of glpFK, which encodes a glycerol diffusion facilitator (glpF) and glycerol kinase (glpK), to E. coli CAG2242 partially prevented the cell death caused by accumulation of spermidine. It was also found that L-glycerol 3-phosphate inhibited spermidine binding to ribosomes and attenuated the inhibition of protein synthesis caused by high concentrations of spermidine. These results indicate that L-glycerol 3-phosphate reduces the binding of excess amounts of spermidine to ribosomes so that protein synthesis is recovered.

* Corresponding author. Mailing address: Graduate School of Pharmaceutical Sciences, Chiba University, 1-33 Yayoi-cho, Inage-ku, Chiba 263-8522, Japan. Phone: 81-43-290-2897. Fax: 81-43-290-2900. E-mail: iga16077{at}p.chiba-u.ac.jp.

Journal of Bacteriology, August 2001, p. 4493-4498, Vol. 183, No. 15
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.15.4493-4498.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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