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J. Biol. Chem., Vol. 277, Issue 20, 17775-17780, May 17, 2002

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Expression of Escherichia coli Glutaredoxin 2 Is Mainly Regulated by ppGpp and ^S*

Aristi Potamitou, Peter Neubauer^§, Arne Holmgren^¶, and Alexios Vlamis-Gardikas

From the  Medical Nobel Institute for Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-171 77 Stockholm, Sweden and the ^§ Bioprocess Engineering Laboratory, Department of Process, Environmental Engineering and Biocenter Oulu, University of Oulu, FIN-90014 Oulu, Finland

Escherichia coli glutaredoxin 2 (Grx2, encoded by grxB) differs greatly from the other two glutaredoxins in structure and catalytic properties. In a wild type strain, levels of Grx2 increased 3-fold in the stationary phase (up to 8 µg/mg). Guanosine-3',5'-tetraphoshate (ppGpp) and ^S, which regulate the transcription of genes in the stationary phase, dramatically affected the expression of Grx2. spoTrelA null mutants, lacking ppGpp, had very low levels of Grx2, while overproduction of full-length RelA or valine-induced starvation of isoleucine, both conditions elevating ppGpp levels, resulted in elevation of Grx2. Null mutants for the ^S-specific protease ClpP, which have higher levels of ^S, exhibited a 3-fold Grx2 increase. ^S in trans also increased the levels of Grx2. Therefore the stationary phase expression of Grx2 is determined by the ^S-bound form of RNA polymerase in connection with ppGpp, while basal levels should be attributed to ⁷⁰-RNA polymerase holoenzyme. Osmotic pressure and cAMP also affected the expression of Grx2, presumably via ^S. Furthermore, Grx2 levels were elevated in an oxyR strain. In accordance with the role of Grx2 as a stationary phase protein, null mutants for grxB were shown to lyse under starvation conditions and exhibited a distorted morphology.

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