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J Biol Chem, Vol. 273, Issue 29, 18382-18388, July 17, 1998
From the We have previously described () that
Escherichia coli maintains a balanced supply of
deoxyribonucleotides by a regulatory mechanism that up-regulates the
levels of ribonucleotide reductase with the lack of its main
hydrogen donors thioredoxin, glutaredoxin 1, and glutathione (GSH). By
using a semi-quantitative reverse transcription/multiplex
polymerase chain reaction fluorescent procedure that enables
simultaneous analysis of up to seven mRNA species, we now
demonstrate that regulation operates at the transcriptional level.
Double mutant cells lacking both thioredoxin and glutaredoxin 1 had
increased transcription of the nrdAB operon, as compared with the corresponding wild type parent (maximal induction of 10- and
9-fold for mRNA of nrdA and nrdB genes,
respectively). Likewise, a dramatic increase of 36-fold in
grxA mRNA was observed in bacteria simultaneously
deficient in thioredoxin and GSH (the physiological reductant of all
glutaredoxins). The increased expression of the grxA gene
in trxA gshA double mutant bacteria was mimicked in
trxA single mutant cells by depletion of GSH with
diethylmaleate (DEM). This induction of grxA transcription
was rapid since maximal increase was detected upon 10 min of DEM
exposure. Like grxA expression, the basal level of
fpg mRNA, encoding formamidopyrimidine-DNA glycosylase,
was increased (about 4-fold) in a trxA gshA double mutant
strain; this expression was also induced upon exposure to DEM (11-fold
maximal induction). These results suggest that transcription of
grxA might share common redox regulatory mechanism(s) with
that of the fpg gene, involved in the repair of
8-oxoguanine in DNA.
In Vivo Transcription of nrdAB Operon and
of grxA and fpg Genes Is Triggered in
Escherichia coli Lacking both Thioredoxin and Glutaredoxin
1 or Thioredoxin and Glutathione, Respectively
,,,, and
Departamento de Bioquímica y
Biología Molecular, Universidad de Córdoba,
14071-Córdoba, España and the ¶ Medical Nobel
Institute for Biochemistry, Department of Medical Biochemistry and
Biophysics, Karolinska Institute, S-171 77, Stockholm, Sweden
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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