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Escherichia coli K-12 substr. MG1655 Polypeptide: dimethyl sulfoxide reductase, chain A



Gene: dmsA Accession Numbers: EG10232 (EcoCyc), b0894, ECK0885

Regulation Summary Diagram: ?

Regulation summary diagram for dmsA

Component of: dimethyl sulfoxide reductase (extended summary available)

Summary:
The DmsA subunit of DMSO reductase contains a molybdo-bis(pyranopterin guanine dinucleotide) (Mo-bisPGD) cofactor and a [4Fe-4S] cluster (known as FS0) [Tang11].

DmsA contains a twin-arginine leader peptide which targets the protein to the membrane, although DmsA does not appear to be exported to the periplasm. The leader peptide is also essential for expression of DmsA and stability of the DmsAB dimer, and is cleaved between residues 45 and 46 [Bilous88, Sambasivarao00]. The leader peptide interacts with the redox enzyme maturation protein (REMP) DmsD [Oresnik01, Chan08, Winstone13].

Gene Citations: [Tseng96, Tseng94]

Locations [Comment 1]: periplasmic space, inner membrane

Map Position: [940,182 -> 942,626] (20.26 centisomes, 73°)
Length: 2445 bp / 814 aa

Molecular Weight of Polypeptide: 90.398 kD (from nucleotide sequence)

pI: 6.53

Unification Links: ASAP:ABE-0003044 , CGSC:17710 , DIP:DIP-9452N , EchoBASE:EB0228 , EcoGene:EG10232 , EcoliWiki:b0894 , Mint:MINT-8046334 , ModBase:P18775 , OU-Microarray:b0894 , PortEco:dmsA , PR:PRO_000022455 , Pride:P18775 , Protein Model Portal:P18775 , RefSeq:NP_415414 , RegulonDB:EG10232 , SMR:P18775 , String:511145.b0894 , UniProt:P18775

Relationship Links: InterPro:IN-FAMILY:IPR006311 , InterPro:IN-FAMILY:IPR006655 , InterPro:IN-FAMILY:IPR006656 , InterPro:IN-FAMILY:IPR006657 , InterPro:IN-FAMILY:IPR006963 , InterPro:IN-FAMILY:IPR009010 , InterPro:IN-FAMILY:IPR011888 , InterPro:IN-FAMILY:IPR019546 , InterPro:IN-FAMILY:IPR027467 , Pfam:IN-FAMILY:PF00384 , Pfam:IN-FAMILY:PF01568 , Pfam:IN-FAMILY:PF04879 , Prosite:IN-FAMILY:PS00490 , Prosite:IN-FAMILY:PS00551 , Prosite:IN-FAMILY:PS00932 , Prosite:IN-FAMILY:PS51318 , Prosite:IN-FAMILY:PS51669 , Smart:IN-FAMILY:SM00926

In Paralogous Gene Group: 222 (14 members)

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Genetic Regulation Schematic: ?

Genetic regulation schematic for dmsA

GO Terms:

Biological Process: GO:0009061 - anaerobic respiration Inferred from experiment [Cotter89]
GO:0006810 - transport Inferred by computational analysis [GOA00]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Chan10, Chan09, Kostecki10]
GO:0009055 - electron carrier activity Inferred from experiment Inferred by computational analysis [GOA01a, Trieber94]
GO:0009389 - dimethyl sulfoxide reductase activity Inferred from experiment Inferred by computational analysis [GOA01a, Sambasivarao91]
GO:0048037 - cofactor binding Inferred from experiment [Tang11]
GO:0051539 - 4 iron, 4 sulfur cluster binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, Tang11]
GO:0003954 - NADH dehydrogenase activity Inferred by computational analysis [Gaudet10]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0030151 - molybdenum ion binding Inferred by computational analysis [GOA01a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
GO:0051536 - iron-sulfur cluster binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0009390 - dimethyl sulfoxide reductase complex Inferred from experiment [Weiner88]
GO:0031237 - intrinsic component of periplasmic side of plasma membrane Inferred from experiment [Stanley02]
GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, Gaudet10]
GO:0030288 - outer membrane-bounded periplasmic space Inferred by computational analysis [Gaudet10]

MultiFun Terms: cell structure membrane
metabolism energy metabolism, carbon anaerobic respiration
metabolism energy production/transport electron acceptors

Essentiality data for dmsA knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 2]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 3]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 4]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 3]
Yes [Feist07, Comment 5]

Credits:
Last-Curated ? 29-Apr-2008 by Nolan L , Macquarie University


Subunit of: dimethyl sulfoxide reductase

Synonyms: DMSO/TMAO reductase, menaquinol:dimethyl sulfoxide oxidoreductase

Subunit composition of dimethyl sulfoxide reductase = [DmsA][DmsB][DmsC]
         dimethyl sulfoxide reductase, chain A = DmsA (summary available)
         dimethyl sulfoxide reductase, chain B = DmsB (summary available)
         dimethyl sulfoxide reductase, chain C = DmsC (summary available)

Summary:
Dimethyl sulfoxide (DMSO) reductase is a membrane-associated Fe-S molybdoenzyme which catalyses the reduction of DMSO to dimethyl sulfide. The enzyme functions as a terminal reductase during anaerobic respiration on DMSO [Bilous85, Bilous88a, Sambasivarao91]. Purified DMSO reductase has broad substrate specificity - it is active on hydroxylamine and chlorate plus a range of amine-N-oxides (including trimethylamine N-oxide ) and methyl-sulfoxides [Weiner88].

DMSO reductase is a member of the complex iron sulfur molybdoenzyme (CISM) family [Rothery08]. The enzyme complex contains three non-identical subunits - a catalytic subunit (DmsA) with a molybdo-bis(pyranopterin guanine dinucleotide) (Mo-bisPGD) cofactor and a [4Fe-4S] cluster (known as FS0), an electron transfer subunit (DmsB) containing four [4Fe-4S] clusters (FS1-FS4) and a membrane anchor subunit (DmsC) containing the quinone-binding site [Weiner88, Cammack90, Trieber94]. Electron transfer is believed to occur from the menaquinol binding site in DmsC, via the Fe-S clusters in DmsB to the site of DMSO reduction in DmsA [Tang11].

Early experiments suggested that the DmsAB subunits were located on the cytoplasmic face of the inner membrane [Sambasivarao91, Rothery93] however later work showed they were present at the the periplasmic face of the inner membrane [Stanley02]. DmsC is the integral membrane subunit - it is required for membrane localization of the complex [Weiner93, Sambasivarao91].

Insertion of the molybdenum cofactor and targeting of the enzyme to the inner membrane requires the redox enzyme maturation protein (REMP), DmsD (reviewed in [Sargent02]).

The enzyme functions anaerobically in the absence of nitrate (a preferred terminal electron acceptor). Anaerobiosis stimulates its expression 100-fold, an effect controlled by the Fnr regulatory protein [Cotter89].

Please note: analysis of DMSO reductase has largely been done using E. coli HB101.

Reviews: [Weiner92]

Citations: [Tang13, Rothery99a, Rothery96, Cheng05, SimalaGrant98]

Locations [Comment 6]: inner membrane

GO Terms:

Biological Process: GO:0009061 - anaerobic respiration Inferred from experiment [Sambasivarao91, Bilous85, Cotter89]
GO:0019645 - anaerobic electron transport chain Inferred from experiment [Bilous85, Bogachev96]
GO:0006810 - transport Inferred by computational analysis [GOA00]
Molecular Function: GO:0009389 - dimethyl sulfoxide reductase activity Inferred by computational analysis Inferred from experiment [Sambasivarao91, Bilous85, Weiner88, GOA01a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment [Sambasivarao91, Weiner88]
GO:0009390 - dimethyl sulfoxide reductase complex Inferred from experiment [Weiner88]
GO:0031237 - intrinsic component of periplasmic side of plasma membrane Inferred from experiment [Stanley02]
GO:0016020 - membrane Inferred by computational analysis [GOA00]

Credits:
Revised 04-Nov-2014 by Mackie A , Macquarie University


Enzymatic reaction of: dimethyl sulfoxide reductase

Synonyms: DMSO reductase

EC Number: 1.8.5.3

Transport reaction diagram for dimethyl sulfoxide reductase

Alternative Substrates for dimethyl sulfoxide [Comment 7 ]: pyridine-N-oxide [Weiner88 ] , nicotinic acid N-oxide [Weiner88 ] , α-picoline N-oxide [Weiner88 ] , hydroxypyridine N-oxide [Weiner88 ] , nicotinamide N-oxide [Weiner88 ] , 3-picoline N-oxide [Weiner88 ] , 4-picoline N-oxide [Weiner88 ] , trimethylamine N-oxide [Weiner88 ] , tetrahydrothiophene 1-oxide [Weiner88 ] , L-methionine S-oxide [Weiner88 ] , methyl phenyl sulfoxide [Weiner88 ] , hydroxylamine [Weiner88 ] , chlorate [Weiner88 ]

In Pathways: NADH to dimethyl sulfoxide electron transfer , formate to dimethyl sulfoxide electron transfer , hydrogen to dimethyl sulfoxide electron transfer

Cofactors or Prosthetic Groups: a [4Fe-4S] iron-sulfur cluster [Cammack90], bis(guanylyl molybdopterin cofactor) [Tang11]

Activators (Unknown Mechanism): Fe2+ [Weiner88]

Kinetic Parameters:

Substrate
Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)
Citations
L-methionine S-oxide
470.0
[Weiner88]
nicotinamide N-oxide
500.0
[Weiner88]
chlorate
7750.0
[Weiner88]
tetrahydrothiophene 1-oxide
600.0
[Weiner88]
4-picoline N-oxide
1000.0
[Weiner88]
dimethyl sulfoxide
180.0
79.9
0.44
[SimalaGrant96, BRENDA14]


Sequence Features

Protein sequence of dimethyl sulfoxide reductase, chain A with features indicated

Feature Class Location Citations Comment
Signal-Sequence 1 -> 45
[Bilous88, UniProt11]
UniProt: Tat-type signal.
Mutagenesis-Variant 17
[Sambasivarao00, UniProt15]
UniProt: Not targeted to the membrane, does not support anaerobic growth.
Chain 46 -> 814
[UniProt09]
UniProt: Anaerobic dimethyl sulfoxide reductase chain A;
Conserved-Region 56 -> 118
[UniProt13]
UniProt: 4Fe-4S Mo/W bis-MGD-type.
Mutagenesis-Variant 57
[Trieber94, UniProt15]
UniProt: No alteration of the growth, expression, or catalytic activities.
Metal-Binding-Site 63
[UniProt10]
UniProt: Iron-sulfur (4Fe-4S); Non-Experimental Qualifier: by similarity;
Mutagenesis-Variant 67
[Rothery99a, Trieber94, UniProt15]
UniProt: Electron transfer from the 4Fe-4S clusters of DmsB to the Mo-bisMGD of DmsA is blocked. Little effect on the coordination sphere of the molybdenum and only minor effects on its redox chemistry.
Metal-Binding-Site 67
[UniProt10]
UniProt: Iron-sulfur (4Fe-4S); Non-Experimental Qualifier: by similarity;
Mutagenesis-Variant 71
[Trieber94, UniProt15]
UniProt: Can not support growth.
Metal-Binding-Site 71
[UniProt10]
UniProt: Iron-sulfur (4Fe-4S); Non-Experimental Qualifier: by similarity;
Mutagenesis-Variant 104
[Trieber94, UniProt15]
UniProt: No alteration of the growth, expression, or catalytic activities.
Metal-Binding-Site 104
[UniProt10]
UniProt: Iron-sulfur (4Fe-4S); Non-Experimental Qualifier: by similarity;
Mutagenesis-Variant 106
[Rothery99a, Trieber94, UniProt15]
UniProt: Electron transfer from the 4Fe-4S clusters of DmsB to the Mo-bisMGD of DmsA is blocked. Little effect on the coordination sphere of the molybdenum and only minor effects on its redox chemistry.
Protein-Segment 172 -> 176
[UniProt12b]
UniProt: Molybdopterin 1 binding; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 205
[UniProt13]
UniProt: Molybdenum; Non-Experimental Qualifier: by similarity.
Protein-Segment 244 -> 245
[UniProt12b]
UniProt: Molybdopterin 2 binding; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: by similarity.
Protein-Segment 270 -> 271
[UniProt12b]
UniProt: Molybdopterin 2 binding; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: by similarity.
Protein-Segment 291 -> 293
[UniProt12b]
UniProt: Molybdopterin 2 binding; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: by similarity.
Protein-Segment 386 -> 387
[UniProt12b]
UniProt: Molybdopterin 2 binding; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: by similarity.
Amino-Acid-Sites-That-Bind 390
[UniProt12b]
UniProt: Molybdopterin 1; Non-Experimental Qualifier: by similarity.
Amino-Acid-Sites-That-Bind 488
[UniProt12b]
UniProt: Molybdopterin 1; Non-Experimental Qualifier: by similarity.
Protein-Segment 512 -> 513
[UniProt12b]
UniProt: Molybdopterin 1 binding; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: by similarity.
Protein-Segment 701
[UniProt12b]
UniProt: Molybdopterin 1 binding; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: by similarity.
Protein-Segment 707 -> 709
[UniProt12b]
UniProt: Molybdopterin 1 binding; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: by similarity.
Amino-Acid-Sites-That-Bind 788
[UniProt12b]
UniProt: Molybdopterin 1; Non-Experimental Qualifier: by similarity.
Protein-Segment 804 -> 805
[UniProt12b]
UniProt: Molybdopterin 1 binding; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: by similarity.


Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Units:

Transcription-unit diagram

Transcription-unit diagram

Notes:

History:
Ingrid Keseler on Thu Mar 3, 2005:
Location of initiating methionine corrected according to Sambasivarao et al., J. Biol. Chem. 275: 22526-22531 (2000).
10/20/97 Gene b0894 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10232; confirmed by SwissProt match.


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Bilous85: Bilous PT, Weiner JH (1985). "Proton translocation coupled to dimethyl sulfoxide reduction in anaerobically grown Escherichia coli HB101." J Bacteriol 163(1);369-75. PMID: 2989249

Bilous88: Bilous PT, Cole ST, Anderson WF, Weiner JH (1988). "Nucleotide sequence of the dmsABC operon encoding the anaerobic dimethylsulphoxide reductase of Escherichia coli." Mol Microbiol 2(6);785-95. PMID: 3062312

Bilous88a: Bilous PT, Weiner JH (1988). "Molecular cloning and expression of the Escherichia coli dimethyl sulfoxide reductase operon." J Bacteriol 170(4);1511-8. PMID: 2832366

Bogachev96: Bogachev AV, Murtazina RA, Skulachev VP (1996). "H+/e- stoichiometry for NADH dehydrogenase I and dimethyl sulfoxide reductase in anaerobically grown Escherichia coli cells." J Bacteriol 178(21);6233-7. PMID: 8892824

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

Cammack90: Cammack R, Weiner JH (1990). "Electron paramagnetic resonance spectroscopic characterization of dimethyl sulfoxide reductase of Escherichia coli." Biochemistry 1990;29(36);8410-6. PMID: 2174699

Chan08: Chan CS, Winstone TM, Chang L, Stevens CM, Workentine ML, Li H, Wei Y, Ondrechen MJ, Paetzel M, Turner RJ (2008). "Identification of residues in DmsD for twin-arginine leader peptide binding, defined through random and bioinformatics-directed mutagenesis." Biochemistry 47(9);2749-59. PMID: 18247574

Chan09: Chan CS, Chang L, Rommens KL, Turner RJ (2009). "Differential interactions between Tat-specific redox enzyme peptides and their chaperones." J Bacteriol 191(7):2091-101. PMID: 19151138

Chan10: Chan CS, Chang L, Winstone TM, Turner RJ (2010). "Comparing system-specific chaperone interactions with their Tat dependent redox enzyme substrates." FEBS Lett 584(22);4553-8. PMID: 20974141

Cheng05: Cheng VW, Rothery RA, Bertero MG, Strynadka NC, Weiner JH (2005). "Investigation of the environment surrounding iron-sulfur cluster 4 of Escherichia coli dimethylsulfoxide reductase." Biochemistry 44(22);8068-77. PMID: 15924426

Cotter89: Cotter PA, Gunsalus RP (1989). "Oxygen, nitrate, and molybdenum regulation of dmsABC gene expression in Escherichia coli." J Bacteriol 171(7);3817-23. PMID: 2544558

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Gaudet10: Gaudet P, Livstone M, Thomas P (2010). "Annotation inferences using phylogenetic trees." PMID: 19578431

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA00: GOA (2000). "Gene Ontology annotation based on Swiss-Prot keyword mapping."

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kostecki10: Kostecki JS, Li H, Turner RJ, DeLisa MP (2010). "Visualizing interactions along the Escherichia coli twin-arginine translocation pathway using protein fragment complementation." PLoS One 5(2);e9225. PMID: 20169075

Oresnik01: Oresnik IJ, Ladner CL, Turner RJ (2001). "Identification of a twin-arginine leader-binding protein." Mol Microbiol 40(2);323-31. PMID: 11309116

Rothery08: Rothery RA, Workun GJ, Weiner JH (2008). "The prokaryotic complex iron-sulfur molybdoenzyme family." Biochim Biophys Acta 1778(9);1897-929. PMID: 17964535

Rothery93: Rothery RA, Weiner JH (1993). "Topological characterization of Escherichia coli DMSO reductase by electron paramagnetic resonance spectroscopy of an engineered [3Fe-4S] cluster." Biochemistry 32(22);5855-61. PMID: 8389193

Rothery96: Rothery RA, Weiner JH (1996). "Interaction of an engineered [3Fe-4S] cluster with a menaquinol binding site of Escherichia coli DMSO reductase." Biochemistry 35(10);3247-57. PMID: 8605160

Rothery99a: Rothery RA, Trieber CA, Weiner JH (1999). "Interactions between the molybdenum cofactor and iron-sulfur clusters of Escherichia coli dimethylsulfoxide reductase." J Biol Chem 274(19);13002-9. PMID: 10224050

Sambasivarao00: Sambasivarao D, Turner RJ, Simala-Grant JL, Shaw G, Hu J, Weiner JH (2000). "Multiple roles for the twin arginine leader sequence of dimethyl sulfoxide reductase of Escherichia coli." J Biol Chem 275(29);22526-31. PMID: 10801884

Sambasivarao90: Sambasivarao D, Scraba DG, Trieber C, Weiner JH (1990). "Organization of dimethyl sulfoxide reductase in the plasma membrane of Escherichia coli." J Bacteriol 1990;172(10);5938-48. PMID: 2170332

Sambasivarao91: Sambasivarao D, Weiner JH (1991). "Dimethyl sulfoxide reductase of Escherichia coli: an investigation of function and assembly by use of in vivo complementation." J Bacteriol 1991;173(19);5935-43. PMID: 1917829

Sargent02: Sargent F, Berks BC, Palmer T (2002). "Assembly of membrane-bound respiratory complexes by the Tat protein-transport system." Arch Microbiol 178(2);77-84. PMID: 12115052

SimalaGrant96: Simala-Grant JL, Weiner JH (1996). "Kinetic analysis and substrate specificity of Escherichia coli dimethyl sulfoxide reductase." Microbiology 142 ( Pt 11);3231-9. PMID: 8969520

SimalaGrant98: Simala-Grant JL, Weiner JH (1998). "Modulation of the substrate specificity of Escherichia coli dimethylsulfoxide reductase." Eur J Biochem 251(1-2);510-5. PMID: 9492325

Stanley02: Stanley NR, Sargent F, Buchanan G, Shi J, Stewart V, Palmer T, Berks BC (2002). "Behaviour of topological marker proteins targeted to the Tat protein transport pathway." Mol Microbiol 43(4);1005-21. PMID: 11929547

Tang11: Tang H, Rothery RA, Voss JE, Weiner JH (2011). "Correct assembly of iron-sulfur cluster FS0 into Escherichia coli dimethyl sulfoxide reductase (DmsABC) is a prerequisite for molybdenum cofactor insertion." J Biol Chem 286(17);15147-54. PMID: 21357619

Tang13: Tang H, Rothery RA, Weiner JH (2013). "A variant conferring cofactor-dependent assembly of Escherichia coli dimethylsulfoxide reductase." Biochim Biophys Acta 1827(6);730-7. PMID: 23481370

Trieber94: Trieber CA, Rothery RA, Weiner JH (1994). "Multiple pathways of electron transfer in dimethyl sulfoxide reductase of Escherichia coli." J Biol Chem 1994;269(10);7103-9. PMID: 8125918

Tseng94: Tseng CP, Hansen AK, Cotter P, Gunsalus RP (1994). "Effect of cell growth rate on expression of the anaerobic respiratory pathway operons frdABCD, dmsABC, and narGHJI of Escherichia coli." J Bacteriol 1994;176(21);6599-605. PMID: 7961411

Tseng96: Tseng CP, Albrecht J, Gunsalus RP (1996). "Effect of microaerophilic cell growth conditions on expression of the aerobic (cyoABCDE and cydAB) and anaerobic (narGHJI, frdABCD, and dmsABC) respiratory pathway genes in Escherichia coli." J Bacteriol 1996;178(4);1094-8. PMID: 8576043

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProt12b: UniProt Consortium (2012). "UniProt version 2012-02 released on 2012-02-29 00:00:00." Database.

UniProt13: UniProt Consortium (2013). "UniProt version 2013-08 released on 2013-08-01 00:00:00." Database.

UniProt15: UniProt Consortium (2015). "UniProt version 2015-01 released on 2015-01-16 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Weiner88: Weiner JH, MacIsaac DP, Bishop RE, Bilous PT (1988). "Purification and properties of Escherichia coli dimethyl sulfoxide reductase, an iron-sulfur molybdoenzyme with broad substrate specificity." J Bacteriol 1988;170(4);1505-10. PMID: 3280546

Weiner92: Weiner JH, Rothery RA, Sambasivarao D, Trieber CA (1992). "Molecular analysis of dimethylsulfoxide reductase: a complex iron-sulfur molybdoenzyme of Escherichia coli." Biochim Biophys Acta 1102(1);1-18. PMID: 1324728

Weiner93: Weiner JH, Shaw G, Turner RJ, Trieber CA (1993). "The topology of the anchor subunit of dimethyl sulfoxide reductase of Escherichia coli." J Biol Chem 268(5);3238-44. PMID: 8429002

Winstone13: Winstone TM, Tran VA, Turner RJ (2013). "The hydrophobic region of the DmsA twin-arginine leader peptide determines specificity with chaperone DmsD." Biochemistry 52(43);7532-41. PMID: 24093457

Other References Related to Gene Regulation

Bearson02: Bearson SM, Albrecht JA, Gunsalus RP (2002). "Oxygen and nitrate-dependent regulation of dmsABC operon expression in Escherichia coli: sites for Fnr and NarL protein interactions." BMC Microbiol 2(1);13. PMID: 12079504

Bradley07: Bradley MD, Beach MB, de Koning AP, Pratt TS, Osuna R (2007). "Effects of Fis on Escherichia coli gene expression during different growth stages." Microbiology 153(Pt 9);2922-40. PMID: 17768236

Lamberg00: Lamberg KE, Kiley PJ (2000). "FNR-dependent activation of the class II dmsA and narG promoters of Escherichia coli requires FNR-activating regions 1 and 3." Mol Microbiol 38(4);817-27. PMID: 11115116

McNicholas98: McNicholas PM, Chiang RC, Gunsalus RP (1998). "Anaerobic regulation of the Escherichia coli dmsABC operon requires the molybdate-responsive regulator ModE." Mol Microbiol 27(1);197-208. PMID: 9466267

Melville96: Melville SB, Gunsalus RP (1996). "Isolation of an oxygen-sensitive FNR protein of Escherichia coli: interaction at activator and repressor sites of FNR-controlled genes." Proc Natl Acad Sci U S A 93(3);1226-31. PMID: 8577745

Pruss01: Pruss BM, Liu X, Hendrickson W, Matsumura P (2001). "FlhD/FlhC-regulated promoters analyzed by gene array and lacZ gene fusions." FEMS Microbiol Lett 2001;197(1);91-7. PMID: 11287152

Tyson93: Tyson KL, Bell AI, Cole JA, Busby SJ (1993). "Definition of nitrite and nitrate response elements at the anaerobically inducible Escherichia coli nirB promoter: interactions between FNR and NarL." Mol Microbiol 1993;7(1);151-7. PMID: 8437517

Zhang13: Zhang HK, Lu H, Wang J, Liu GF, Zhou JT, Xu MY (2013). "Global transcriptome analysis of Escherichia coli exposed to immobilized anthraquinone-2-sulfonate and azo dye under anaerobic conditions." Appl Microbiol Biotechnol 97(15);6895-905. PMID: 23820558


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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