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Papers In Press, published online ahead of print March 13, 2002
Medical Nobel Institute for Biochemistry, Karolinska Institutet, Stockholm S-171 77
Corresponding Author: Arne.Holmgren{at}mbb.ki.se
Levels of Escherichia coli thioredoxin 1 (Trx1), thioredoxin 2 (Trx2), glutaredoxin 1 (Grx1), glutaredoxin 2 (Grx2) and glutaredoxin 3 (Grx3) have been determined by novel sensitive ELISA methods. In a wild type strain, Trx1 levels increased from exponential to stationary phase of growth (1.5-fold to 3400 ng/mg), as did the levels of Grx2 (from ~2500 ng/mg to ~8000 ng/mg). Grx3 and Trx2 levels were quite stable during growth (~4500 ng/mg and ~200 ng/mg respectively). Grx1 levels decreased from ~600 ng/mg at the exponential phase to ~285 ng/mg at the stationary phase. A large elevation of Grx1 (20-30-fold) was observed in null mutants for the thioredoxin system while levels of the other redoxins in all combinations of examined null mutants barely exceeded a 2 to 3-fold increase. Measurements of thymidine incorporation in newly synthesized DNA suggested that mainly Grx1 and to a lesser extent Trx1 contribute to the reduction of ribonucleotides. All glutaredoxin species were elevated in catalase deficient strains, implying an antioxidant role for the glutaredoxins. Trx1, Trx2 and Grx1 levels increased after exposure to hydrogen peroxide and decreased after exposure to mercaptoethanol. Levels of Grx2 and Grx3 behaved exactly the opposite, suggesting that OxyR does not regulate their expression.
J. Biol. Chem, 10.1074/jbc.M201225200
Submitted on February 6, 2002
Revised on March 13, 2002
Accepted on March 12, 2002
Protein levels of Escherichia coli thioredoxins and glutaredoxins and their realtion to null mutants, growth phase and function
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