RegulonDB

Gene
Name:	grxA
Synonym(s):	ECK0840, EG10417, b0849, grx
Genome position(nucleotides):	890496 <-- 890753 Genome Browser
Strand:	reverse
Sequence:	Get nucleotide sequence FastaFormat
GC content %:	44.96
External database links:

ASAP:	ABE-0002893
CGSC:	17683
ECHOBASE:	EB0412
ECOLIHUB:	grxA
OU-MICROARRAY:	b0849
STRING:	511145.b0849
COLOMBOS:	grxA

Transcriptional Regulation
	Display Regulation
Activated by:	OxyR

Reference(s)
[1] Aberg A., Hahne S., Karlsson M., Larsson A., Ormo M., Ahgren A., Sjoberg BM., 1989, Evidence for two different classes of redox-active cysteines in ribonucleotide reductase of Escherichia coli., J Biol Chem 264(21):12249-52
[2] Allner O., Foloppe N., Nilsson L., 2015, Motions and entropies in proteins as seen in NMR relaxation experiments and molecular dynamics simulations., J Phys Chem B 119(3):1114-28
[3] Bhomkar P., Materi W., Semenchenko V., Wishart DS., 2010, Transcriptional response of E. coli upon FimH-mediated fimbrial adhesion., Gene Regul Syst Bio 4:1-17
[4] Casi G., Roelfes G., Hilvert D., 2008, Selenoglutaredoxin as a glutathione peroxidase mimic., Chembiochem 9(10):1623-31
[5] Cole R., Loria JP., 2003, FAST-Modelfree: a program for rapid automated analysis of solution NMR spin-relaxation data., J Biomol NMR 26(3):203-13
[6] Daer S., Goodwill JE., Ikuma K., 2020, Effect of ferrate and monochloramine disinfection on the physiological and transcriptomic response of Escherichia coli at late stationary phase., Water Res 189:116580
[7] Dyson HJ., 1995, Nuclear magnetic resonance of thioredoxin and glutaredoxin., Methods Enzymol 252:293-306
[8] Eklund H., Cambillau C., Sjoberg BM., Holmgren A., Jornvall H., Hoog JO., Branden CI., 1984, Conformational and functional similarities between glutaredoxin and thioredoxins., EMBO J 3(7):1443-9
[9] Eser M., Masip L., Kadokura H., Georgiou G., Beckwith J., 2009, Disulfide bond formation by exported glutaredoxin indicates glutathione's presence in the E. coli periplasm., Proc Natl Acad Sci U S A 106(5):1572-7
[10] Fernandes AP., Fladvad M., Berndt C., Andresen C., Lillig CH., Neubauer P., Sunnerhagen M., Holmgren A., Vlamis-Gardikas A., 2005, A novel monothiol glutaredoxin (Grx4) from Escherichia coli can serve as a substrate for thioredoxin reductase., J Biol Chem 280(26):24544-52
[11] Fetrow JS., Godzik A., Skolnick J., 1998, Functional analysis of the Escherichia coli genome using the sequence-to-structure-to-function paradigm: identification of proteins exhibiting the glutaredoxin/thioredoxin disulfide oxidoreductase activity., J Mol Biol 282(4):703-11
[12] Flandrin A., Allouche S., Rolland Y., McDuff FO., Richard Wagner J., Klarskov K., 2015, Characterization of dehydroascorbate-mediated modification of glutaredoxin by mass spectrometry., J Mass Spectrom 50(12):1358-66
[13] Fuchs JA., 1995, Glutathione mutants., Methods Enzymol 252:83-92
[14] Gelhaye E., Rouhier N., Jacquot JP., 2003, Evidence for a subgroup of thioredoxin h that requires GSH/Grx for its reduction., FEBS Lett 555(3):443-8
[15] Harrison JJ., Tremaroli V., Stan MA., Chan CS., Vacchi-Suzzi C., Heyne BJ., Parsek MR., Ceri H., Turner RJ., 2009, Chromosomal antioxidant genes have metal ion-specific roles as determinants of bacterial metal tolerance., Environ Microbiol 11(10):2491-509
[16] Holmgren A., 1988, Thioredoxin and glutaredoxin: small multi-functional redox proteins with active-site disulphide bonds., Biochem Soc Trans 16(2):95-6
[17] Holmgren A., 1979, Glutathione-dependent synthesis of deoxyribonucleotides. Characterization of the enzymatic mechanism of Escherichia coli glutaredoxin., J Biol Chem 254(9):3672-8
[18] Holmgren A., 1979, Glutathione-dependent synthesis of deoxyribonucleotides. Purification and characterization of glutaredoxin from Escherichia coli., J Biol Chem 254(9):3664-71
[19] Holmgren A., 1985, Glutaredoxin from Escherichia coli and calf thymus., Methods Enzymol 113:525-40
[20] Holmgren A., Aslund F., 1995, Glutaredoxin., Methods Enzymol 252:283-92
[21] Hoog JO., Douglas KT., D'Silva C., Holmgren A., 1982, Photo-labelling of glutaredoxin from Escherichia coli., Biochem Biophys Res Commun 107(4):1475-81
[22] Hoog JO., Holmgren A., D'Silva C., Douglas KT., Seddon AP., 1982, Glutathione derivatives as inhibitors of glutaredoxin and ribonucleotide reductase from Escherichia coli., FEBS Lett 138(1):59-61
[23] Hoog JO., von Bahr-Lindstrom H., Jornvall H., Holmgren A., 1986, Cloning and expression of the glutaredoxin (grx) gene of Escherichia coli., Gene 43(1-2):13-21
[24] Lillig CH., Potamitou A., Schwenn JD., Vlamis-Gardikas A., Holmgren A., 2003, Redox regulation of 3'-phosphoadenylylsulfate reductase from Escherichia coli by glutathione and glutaredoxins., J Biol Chem 278(25):22325-30
[25] Liu J., Rosen BP., 1997, Ligand interactions of the ArsC arsenate reductase., J Biol Chem 272(34):21084-9
[26] Luginbuhl P., Guntert P., Billeter M., Wuthrich K., 1996, The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules., J Biomol NMR 8(2):136-46
[27] Lundstrom-Ljung J., Holmgren A., 1995, Glutaredoxin accelerates glutathione-dependent folding of reduced ribonuclease A together with protein disulfide-isomerase., J Biol Chem 270(14):7822-8
[28] Lundstrom-Ljung J., Vlamis-Gardikas A., Aslund F., Holmgren A., 1999, Reactivity of glutaredoxins 1, 2 and 3 from Escherichia coli and protein disulfide isomerase towards glutathionyl-mixed disulfides in ribonuclease A., FEBS Lett 443(2):85-8
[29] Miranda-Vizuete A., Martinez-Galisteo E., Aslund F., Lopez-Barea J., Pueyo C., Holmgren A., 1994, Null thioredoxin and glutaredoxin Escherichia coli K-12 mutants have no enhanced sensitivity to mutagens due to a new GSH-dependent hydrogen donor and high increases in ribonucleotide reductase activity., J Biol Chem 269(24):16631-7
[30] Nagahara N., 2020, Activation of 3-Mercaptopyruvate Sulfurtransferase by Glutaredoxin Reducing System., Biomolecules 10(6)
[31] Nygren H., Rozell B., Holmgren A., Hansson HA., 1981, Immunoelectron microscopic localization of glutaredoxin and thioredoxin in Escherichia coli cells., FEBS Lett 133(1):145-50
[32] Parsonage D., Reeves SA., Karplus PA., Poole LB., 2010, Engineering of fluorescent reporters into redox domains to monitor electron transfers., Methods Enzymol 474:1-21
[33] Porras P., Pedrajas JR., Martinez-Galisteo E., Padilla CA., Johansson C., Holmgren A., Barcena JA., 2002, Glutaredoxins catalyze the reduction of glutathione by dihydrolipoamide with high efficiency., Biochem Biophys Res Commun 295(5):1046-51
[34] Pueyo C., Jurado J., Prieto-Alamo MJ., Monje-Casas F., Lopez-Barea J., 2002, Multiplex reverse transcription-polymerase chain reaction for determining transcriptional regulation of thioredoxin and glutaredoxin pathways., Methods Enzymol 347:441-51
[35] Shi J., Vlamis-Gardikas A., Aslund F., Holmgren A., Rosen BP., 1999, Reactivity of glutaredoxins 1, 2, and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction., J Biol Chem 274(51):36039-42
[36] Smirnova G., Muzyka N., Lepekhina E., Oktyabrsky O., 2016, Roles of the glutathione- and thioredoxin-dependent systems in the Escherichia coli responses to ciprofloxacin and ampicillin., Arch Microbiol 198(9):913-21
[37] Ukuwela AA., Bush AI., Wedd AG., Xiao Z., 2017, Reduction potentials of protein disulfides and catalysis of glutathionylation and deglutathionylation by glutaredoxin enzymes., Biochem J 474(22):3799-3815
[38] Uria-Nickelsen MR., Leadbetter ER., Godchaux W., 1993, Sulphonate utilization by enteric bacteria., J Gen Microbiol 139(2):203-8
[39] Vlamis-Gardikas A., Holmgren A., 2002, Thioredoxin and glutaredoxin isoforms., Methods Enzymol 347:286-96
[40] Vrionis HA., Wang S., Haslam B., Turner RJ., 2015, Selenite Protection of Tellurite Toxicity Toward Escherichia coli., Front Mol Biosci 2:69
[41] Wurfel M., Haberlein I., Follmann H., 1993, Facile sulfitolysis of the disulfide bonds in oxidized thioredoxin and glutaredoxin., Eur J Biochem 211(3):609-14