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Escherichia coli K-12 substr. MG1655 Polypeptide: DNA gyrase, subunit B

Gene: gyrB Accession Numbers: EG10424 (EcoCyc), b3699, ECK3691

Synonyms: cou, hopA, pcpA, pcbA, parA, nalC, Cou, acrB, himB, hisU

Regulation Summary Diagram

Regulation summary diagram for gyrB

Component of: DNA gyrase (extended summary available)

The GyrB subunit of DNA gyrase is required for the ATPase activity of the enzyme. Novobiocin and other coumarin antibiotics are competitive inhibitors of the ATPase activity [Staudenbauer81].

GyrB contains a sizeable insert sequence in its TOPRIM domain that is present in many gram-negative bacteria but not common in other organisms. A crystal structure to 3.1 Å resolution of a GyrBA fusion suggests that this insert "braces" the TOPRIM domain in GyrB against its binding surface in GyrA. Deletion analysis shows that this region is critical for positive and negative supercoiling, and although it does not bind DNA, is required for DNA binding by GyrB [Schoeffler10].

A gyrBpriA double null is inviable [Grompone03].

Gene Citations: [Adachi84]

Locations: bacterial nucleoid, cytosol

Map Position: [3,875,728 <- 3,878,142] (83.53 centisomes, 301°)
Length: 2415 bp / 804 aa

Molecular Weight of Polypeptide: 89.95 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0012093, CGSC:650, DIP:DIP-48005N, EchoBASE:EB0419, EcoGene:EG10424, EcoliWiki:b3699, OU-Microarray:b3699, PortEco:gyrB, PR:PRO_000022856, Pride:P0AES6, Protein Model Portal:P0AES6, RefSeq:YP_026241, RegulonDB:EG10424, SMR:P0AES6, String:511145.b3699, Swiss-Model:P0AES6, UniProt:P0AES6

Relationship Links: InterPro:IN-FAMILY:IPR001241, InterPro:IN-FAMILY:IPR002288, InterPro:IN-FAMILY:IPR003594, InterPro:IN-FAMILY:IPR006171, InterPro:IN-FAMILY:IPR011557, InterPro:IN-FAMILY:IPR013506, InterPro:IN-FAMILY:IPR013759, InterPro:IN-FAMILY:IPR013760, InterPro:IN-FAMILY:IPR014721, InterPro:IN-FAMILY:IPR018522, InterPro:IN-FAMILY:IPR020568, PDB:Structure:1AJ6, PDB:Structure:1EI1, PDB:Structure:1KZN, PDB:Structure:3G7E, PDB:Structure:3NUH, PDB:Structure:4DUH, PDB:Structure:4HYP, PDB:Structure:4KFG, PDB:Structure:4PRV, PDB:Structure:4PRX, PDB:Structure:4PU9, PDB:Structure:4WUB, PDB:Structure:4WUC, PDB:Structure:4WUD, PDB:Structure:4XTJ, Pfam:IN-FAMILY:PF00204, Pfam:IN-FAMILY:PF00986, Pfam:IN-FAMILY:PF01751, Pfam:IN-FAMILY:PF02518, Prints:IN-FAMILY:PR00418, Prosite:IN-FAMILY:PS00177, Prosite:IN-FAMILY:PS50880, Smart:IN-FAMILY:SM00387, Smart:IN-FAMILY:SM00433

In Paralogous Gene Group: 480 (2 members)

Gene-Reaction Schematic

Gene-Reaction Schematic

Genetic Regulation Schematic

Genetic regulation schematic for gyrB

GO Terms:
Biological Process:
Inferred from experimentInferred by computational analysisGO:0006265 - DNA topological change [GOA01a, Steck84]
Inferred from experimentGO:0006351 - transcription, DNA-templated [Peter04]
Inferred from experimentGO:0042493 - response to drug [Tsai97]
Inferred by computational analysisGO:0006261 - DNA-dependent DNA replication [GOA06]
Inferred by computational analysisGO:0006268 - DNA unwinding involved in DNA replication [Gaudet10]
Inferred by computational analysisGO:0007059 - chromosome segregation [Gaudet10]
Inferred by computational analysisGO:0046677 - response to antibiotic [UniProtGOA11a]
Molecular Function:
Inferred from experimentInferred by computational analysisGO:0003677 - DNA binding [UniProtGOA11a, GOA06, GOA01a, Higgins82, Chatterji00]
Inferred from experimentInferred by computational analysisGO:0003918 - DNA topoisomerase type II (ATP-hydrolyzing) activity [GOA06, GOA01, GOA01a, Sugino78]
Inferred from experimentGO:0005515 - protein binding [Butland05]
Inferred from experimentInferred by computational analysisGO:0005524 - ATP binding [UniProtGOA11a, GOA06, GOA01a, Kampranis98]
Inferred from experimentGO:0008094 - DNA-dependent ATPase activity [Maxwell84]
Inferred by computational analysisGO:0000166 - nucleotide binding [UniProtGOA11a]
Inferred by computational analysisGO:0000287 - magnesium ion binding [GOA06]
Inferred by computational analysisGO:0003916 - DNA topoisomerase activity [UniProtGOA11a]
Inferred by computational analysisGO:0016853 - isomerase activity [UniProtGOA11a]
Inferred by computational analysisGO:0046872 - metal ion binding [UniProtGOA11a]
Cellular Component:
Inferred from experimentInferred by computational analysisGO:0005737 - cytoplasm [UniProtGOA11, UniProtGOA11a, GOA06, Thornton94]
Inferred from experimentInferred by computational analysisGO:0005829 - cytosol [DiazMejia09, Ishihama08, LopezCampistrou05]
Inferred from experimentGO:0009330 - DNA topoisomerase complex (ATP-hydrolyzing) [Higgins78a]
Inferred by computational analysisGO:0005694 - chromosome [GOA01a]
Inferred by computational analysisGO:0009295 - nucleoid [Gaudet10]

MultiFun Terms: information transferDNA relatedDNA replication
information transferRNA relatedTranscription related

Essentiality data for gyrB knockouts:

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB LennoxNo 37 Aerobic 7   No [Baba06, Comment 1]

Subunit of: DNA gyrase

Synonyms: Topoisomerase II

Subunit composition of DNA gyrase = [GyrA]2[GyrB]2
         DNA gyrase, subunit A = GyrA
         DNA gyrase, subunit B = GyrB (summary available)

DNA gyrase is one of two essential members of the type II topoisomerase family in E. coli. It carries out ATP-dependent supercoiling of chromosomal DNA, as well as potentially being involved in decatenation of newly synthesized chrosomal and plasmid DNA.

Gyrase consists of 2 GyrA and 2 GyrB subunits [Sugino80]. The GyrA amino-termini form a dimeric core flanked by their carboxy-terminal domains, which form spirals that wrap the target DNA [Costenaro05, Ruthenburg05]. These GyrA carboxy-terminal domains impart unidirectionality on gyrase supercoiling activity [Ruthenburg05]. The GyrB amino-terminal domain contains the gyrase ATPase activity and is the binding site for antibiotics that inhibit gyrase function [Ali93, Lewis96]. GyrB dimerizes in a "V" shape, with the amino-termini coming together at the base to form the 20 Å ATP-operated DNA-binding clamp and the carboxy-termini at the ends of the "V" involved in protein-protein interaction [Wigley91, Celia94, Brino00, Williams01]. Other studies of the full gyrase tetramer have been carried out in the presence and absence of bound substrate [Krueger90, Sissi05, Blandamer94, Morais97].

Gyrase supercoils and relaxes DNA by cleaving one duplex strand entirely and passing the other, intact DNA duplex through it. The initial gyrase cleavage leaves a staggered cut with 5' overhangs, which romain covalently attached to the GyrA subunits throughout strand transfer [Morrison79]. Indeed, inhibiting the gyrase ATPase stalls the reaction in the middle, yielding double-strand breaks with GyrA monomers attached to each 5' overhang [Sugino80, Gellert79]. DNA supercoiling appears to operate through a two-gate mechanism in which the non-cleaved DNA strand is loaded into the amino-terminal, ATP-dependent clamp formed by dimerized GyrB and then passed through the gap in the bound, cleaved strand [Williams99, Kampranis99]. When this clamp domain is experimentally locked in the closed conformation, gyrase is no longer able to supercoil DNA, but can still carry out a single relaxation reaction [Williams01]. Each round of supercoiling represents a calculated free energy change of 2.6 kJ/mol and requires ATP [Cullis92, Sugino80a]. The mechanics of gyrase function, including its response to tension in DNA, have been examined at the molecular level [Gore06].

In addition to supercoiling and relaxing DNA, gyrase can also separate catenated DNA, straighten knotted DNA and act in deletion of a region flanked by direct repeats [Marians87, Mizuuchi80, MiuraMasuda90].

Gyrase activity is required for DNA synthesis and replication fork progression [Fairweather80, Khodursky00, Smelkova01].

Gyrase binds a 120-bp area, with DNA apparently wrapped around the enzyme [Fisher81]. The minimum duplex length for gyrase action is about half that, at 50-60 bp, although it is much less efficient at this length [Belotserkovskii06]. Although there are no canonical cleavage sequences for gyrase, a TG doublet is present at most cut sites [Morrison79]. In addition, gyrase binds to repetitive extragenic palindromic (REP) sequences 10 times more effectively than to random DNA [Yang88a].

Gyrase activity is halted by the toxic plasmid-encoded protein CcdB, which interacts with GyrA to wedge gyrase open, locking it in its ATP-bound form [Kampranis99a, DaoThi05, Smith06a]. A crystal structure of CcdB has been determined [Loris99].

Gyrase supercoiling activity is regulated by the inhibitor protein GyrI; for more information, see DNA gyrase inhibitor. Glutamate racemase also modulates gyrase supercoiling activity [Ashiuchi02].

Locations: cytosol

GO Terms:
Cellular Component:
GO:0005829 - cytosol []

Last-Curated 20-Mar-2006 by Shearer A, SRI International

Enzymatic reaction of: gyrase

Inferred from experiment

EC Number:

a double stranded DNA + ATP ⇄ a negatively supercoiled DNA + ADP + phosphate

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

Reversibility of this reaction is unspecified.

Cofactors or Prosthetic Groups: Mg2+ [Gellert76]

Kinetic Parameters:
Substrate Km (μM) Citations
ATP 300.0 [Higgins78a]

Sequence Features

Protein sequence of DNA gyrase, subunit B with features indicated

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
Author statement[UniProt15]
UniProt: Removed.
Chain 2 -> 804
Author statement[UniProt15]
UniProt: DNA gyrase subunit B.
Sequence-Conflict 385
Inferred by curator[Burland93, UniProt15]
UniProt: (in Ref. 4; AAA62050).
Conserved-Region 418 -> 533
Inferred by computational analysis[UniProt15]
UniProt: Toprim.
Mutagenesis-Variant 424
Inferred from experiment[Noble02]
E → A or Q: Strongly reduced activity regarding both DNA supercoiling and relaxation. Reduces ATP hydrolysis in response to DNA binding, but has only minor effect on the basal rate of ATP hydrolysis.
Metal-Binding-Site 424
Inferred by computational analysis[UniProt15]
UniProt: Magnesium 1; catalytic.
Metal-Binding-Site 424, 498, 500, 502
These residues are thought to coordinate the one or two divalent magnesium ions required for the gyrase cleavage-religation reaction.
Extrinsic-Sequence-Variant 426
Author statement[UniProt15]
UniProt: In nal-24, nal-102, nal-103, nal-107, nal-108, nal-111, nal-114, en-2 and en-5 mutants; resistant to nalidixic acid and to enoxacin..
Sequence-Conflict 436
Inferred by curator[Funatsuki97, UniProt15]
UniProt: (in Ref. 3; BAA20341).
Extrinsic-Sequence-Variant 447
Author statement[UniProt15]
UniProt: In nal-31, nal-109, nal-115 and nal-120 mutants; resistant to nalidixic acid..
Amino-Acid-Site 449
Inferred by computational analysis[UniProt15]
UniProt: Interaction with DNA; Sequence Annotation Type: site.
Amino-Acid-Site 452
Inferred by computational analysis[UniProt15]
UniProt: Interaction with DNA; Sequence Annotation Type: site.
Mutagenesis-Variant 498
Inferred from experiment[Noble02]
D → A or N: Strongly reduced activity regarding both DNA supercoiling and relaxation. Reduces ATP hydrolysis in response to DNA binding, but has only minor effect on the basal rate of ATP hydrolysis.
Metal-Binding-Site 498
Inferred by computational analysis[UniProt15]
UniProt: Magnesium 1; catalytic.
Mutagenesis-Variant 500
Inferred from experiment[Noble02]
UniProt: Strongly reduced activity regarding both DNA supercoiling and relaxation. Reduces ATP hydrolysis in response to DNA binding, but has only minor effect on the basal rate of ATP hydrolysis.
Metal-Binding-Site 500
Inferred by computational analysis[UniProt15]
UniProt: Magnesium 2.
Mutagenesis-Variant 502
Inferred from experiment[Noble02]
UniProt: Strongly reduced activity regarding both DNA supercoiling and relaxation. Reduces ATP hydrolysis in response to DNA binding, but has only minor effect on the basal rate of ATP hydrolysis.
Extrinsic-Sequence-Variant 751
Author statement[UniProt15]
UniProt: In B17 resistant mutant..
Extrinsic-Sequence-Variant 759 -> 760
Author statement[UniProt15]
UniProt: In acriflavine susceptible mutant..

Sequence Pfam Features

Protein sequence of DNA gyrase, subunit B with features indicated

Feature Class Location Citations Comment
Pfam PF02518 32 -> 173
Inferred by computational analysis[Finn14]
HATPase_c : Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
Pfam PF00204 221 -> 390
Inferred by computational analysis[Finn14]
DNA_gyraseB : DNA gyrase B
Pfam PF01751 419 -> 531
Inferred by computational analysis[Finn14]
Toprim : Toprim domain
Pfam PF00986 732 -> 793
Inferred by computational analysis[Finn14]
DNA_gyraseB_C : DNA gyrase B subunit, carboxyl terminus

Gene Local Context (not to scale -- see Genome Browser for correct scale)

Gene local context diagram

Transcription Unit

Transcription-unit diagram


10/20/97 Gene b3699 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10424; confirmed by SwissProt match.


Adachi84: Adachi T, Mizuuchi K, Menzel R, Gellert M (1984). "DNA sequence and transcription of the region upstream of the E. coli gyrB gene." Nucleic Acids Res 1984;12(16);6389-95. PMID: 6089112

Ali93: Ali JA, Jackson AP, Howells AJ, Maxwell A (1993). "The 43-kilodalton N-terminal fragment of the DNA gyrase B protein hydrolyzes ATP and binds coumarin drugs." Biochemistry 32(10);2717-24. PMID: 8383523

Ashiuchi02: Ashiuchi M, Kuwana E, Yamamoto T, Komatsu K, Soda K, Misono H (2002). "Glutamate racemase is an endogenous DNA gyrase inhibitor." J Biol Chem 277(42);39070-3. PMID: 12213801

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

Belotserkovskii06: Belotserkovskii BP, Arimondo PB, Cozzarelli NR (2006). "Topoisomerase action on short DNA duplexes reveals requirements for gate and transfer DNA segments." J Biol Chem 281(35);25407-15. PMID: 16798730

Blandamer94: Blandamer MJ, Briggs B, Cullis PM, Jackson AP, Maxwell A, Reece RJ (1994). "Domain structure of Escherichia coli DNA gyrase as revealed by differential scanning calorimetry." Biochemistry 33(24);7510-6. PMID: 8011616

Brino00: Brino L, Urzhumtsev A, Mousli M, Bronner C, Mitschler A, Oudet P, Moras D (2000). "Dimerization of Escherichia coli DNA-gyrase B provides a structural mechanism for activating the ATPase catalytic center." J Biol Chem 275(13);9468-75. PMID: 10734094

Burland93: Burland V, Plunkett G, Daniels DL, Blattner FR (1993). "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication." Genomics 1993;16(3);551-61. PMID: 7686882

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Celia94: Celia H, Hoermann L, Schultz P, Lebeau L, Mallouh V, Wigley DB, Wang JC, Mioskowski C, Oudet P (1994). "Three-dimensional model of Escherichia coli gyrase B subunit crystallized in two-dimensions on novobiocin-linked phospholipid films." J Mol Biol 236(2);618-28. PMID: 8107146

Chatterji00: Chatterji M, Unniraman S, Maxwell A, Nagaraja V (2000). "The additional 165 amino acids in the B protein of Escherichia coli DNA gyrase have an important role in DNA binding." J Biol Chem 275(30);22888-94. PMID: 10764756

Costenaro05: Costenaro L, Grossmann JG, Ebel C, Maxwell A (2005). "Small-angle X-ray scattering reveals the solution structure of the full-length DNA gyrase a subunit." Structure 13(2);287-96. PMID: 15698572

Cullis92: Cullis PM, Maxwell A, Weiner DP (1992). "Energy coupling in DNA gyrase: a thermodynamic limit to the extent of DNA supercoiling." Biochemistry 31(40);9642-6. PMID: 1327123

DaoThi05: Dao-Thi MH, Van Melderen L, De Genst E, Afif H, Buts L, Wyns L, Loris R (2005). "Molecular basis of gyrase poisoning by the addiction toxin CcdB." J Mol Biol 348(5);1091-102. PMID: 15854646

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Fairweather80: Fairweather NF, Orr E, Holland IB (1980). "Inhibition of deoxyribonucleic acid gyrase: effects on nucleic acid synthesis and cell division in Escherichia coli K-12." J Bacteriol 142(1);153-61. PMID: 6154685

Finn14: Finn RD, Bateman A, Clements J, Coggill P, Eberhardt RY, Eddy SR, Heger A, Hetherington K, Holm L, Mistry J, Sonnhammer EL, Tate J, Punta M (2014). "Pfam: the protein families database." Nucleic Acids Res 42(Database issue);D222-30. PMID: 24288371

Fisher81: Fisher LM, Mizuuchi K, O'Dea MH, Ohmori H, Gellert M (1981). "Site-specific interaction of DNA gyrase with DNA." Proc Natl Acad Sci U S A 78(7);4165-9. PMID: 6270661

Funatsuki97: Funatsuki K, Tanaka R, Inagaki S, Konno H, Katoh K, Nakamura H (1997). "acrB mutation located at carboxyl-terminal region of gyrase B subunit reduces DNA binding of DNA gyrase." J Biol Chem 272(20);13302-8. PMID: 9148951

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

Gellert76: Gellert M, Mizuuchi K, O'Dea MH, Nash HA (1976). "DNA gyrase: an enzyme that introduces superhelical turns into DNA." Proc Natl Acad Sci U S A 73(11);3872-6. PMID: 186775

Gellert79: Gellert M, Fisher LM, O'Dea MH (1979). "DNA gyrase: purification and catalytic properties of a fragment of gyrase B protein." Proc Natl Acad Sci U S A 76(12);6289-93. PMID: 230505

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

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

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Gore06: Gore J, Bryant Z, Stone MD, Nollmann M, Cozzarelli NR, Bustamante C (2006). "Mechanochemical analysis of DNA gyrase using rotor bead tracking." Nature 439(7072);100-4. PMID: 16397501

Grompone03: Grompone G, Ehrlich SD, Michel B (2003). "Replication restart in gyrB Escherichia coli mutants." Mol Microbiol 48(3);845-54. PMID: 12694626

Higgins78a: Higgins NP, Peebles CL, Sugino A, Cozzarelli NR (1978). "Purification of subunits of Escherichia coli DNA gyrase and reconstitution of enzymatic activity." Proc Natl Acad Sci U S A 75(4);1773-7. PMID: 347446

Higgins82: Higgins NP, Cozzarelli NR (1982). "The binding of gyrase to DNA: analysis by retention by nitrocellulose filters." Nucleic Acids Res 10(21);6833-47. PMID: 6294616

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Kampranis98: Kampranis SC, Maxwell A (1998). "Hydrolysis of ATP at only one GyrB subunit is sufficient to promote supercoiling by DNA gyrase." J Biol Chem 273(41);26305-9. PMID: 9756859

Kampranis99: Kampranis SC, Bates AD, Maxwell A (1999). "A model for the mechanism of strand passage by DNA gyrase." Proc Natl Acad Sci U S A 96(15);8414-9. PMID: 10411889

Kampranis99a: Kampranis SC, Howells AJ, Maxwell A (1999). "The interaction of DNA gyrase with the bacterial toxin CcdB: evidence for the existence of two gyrase-CcdB complexes." J Mol Biol 293(3);733-44. PMID: 10543963

Khodursky00: Khodursky AB, Peter BJ, Schmid MB, DeRisi J, Botstein D, Brown PO, Cozzarelli NR (2000). "Analysis of topoisomerase function in bacterial replication fork movement: use of DNA microarrays." Proc Natl Acad Sci U S A 97(17);9419-24. PMID: 10944214

Krueger90: Krueger S, Zaccai G, Wlodawer A, Langowski J, O'Dea M, Maxwell A, Gellert M (1990). "Neutron and light-scattering studies of DNA gyrase and its complex with DNA." J Mol Biol 211(1);211-20. PMID: 2153834

Lewis96: Lewis RJ, Singh OM, Smith CV, Skarzynski T, Maxwell A, Wonacott AJ, Wigley DB (1996). "The nature of inhibition of DNA gyrase by the coumarins and the cyclothialidines revealed by X-ray crystallography." EMBO J 15(6);1412-20. PMID: 8635474

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Loris99: Loris R, Dao-Thi MH, Bahassi EM, Van Melderen L, Poortmans F, Liddington R, Couturier M, Wyns L (1999). "Crystal structure of CcdB, a topoisomerase poison from E. coli." J Mol Biol 285(4);1667-77. PMID: 9917404

Marians87: Marians KJ (1987). "DNA gyrase-catalyzed decatenation of multiply linked DNA dimers." J Biol Chem 262(21);10362-8. PMID: 3038875

Maxwell84: Maxwell A, Gellert M (1984). "The DNA dependence of the ATPase activity of DNA gyrase." J Biol Chem 259(23);14472-80. PMID: 6094559

MiuraMasuda90: Miura-Masuda A, Ikeda H (1990). "The DNA gyrase of Escherichia coli participates in the formation of a spontaneous deletion by recA-independent recombination in vivo." Mol Gen Genet 220(3);345-52. PMID: 2160049

Mizuuchi80: Mizuuchi K, Fisher LM, O'Dea MH, Gellert M (1980). "DNA gyrase action involves the introduction of transient double-strand breaks into DNA." Proc Natl Acad Sci U S A 77(4);1847-51. PMID: 6246508

Morais97: Morais Cabral JH, Jackson AP, Smith CV, Shikotra N, Maxwell A, Liddington RC (1997). "Crystal structure of the breakage-reunion domain of DNA gyrase." Nature 388(6645);903-6. PMID: 9278055

Morrison79: Morrison A, Cozzarelli NR (1979). "Site-specific cleavage of DNA by E. coli DNA gyrase." Cell 17(1);175-84. PMID: 378403

Noble02: Noble CG, Maxwell A (2002). "The role of GyrB in the DNA cleavage-religation reaction of DNA gyrase: a proposed two metal-ion mechanism." J Mol Biol 318(2);361-71. PMID: 12051843

Peter04: Peter BJ, Arsuaga J, Breier AM, Khodursky AB, Brown PO, Cozzarelli NR (2004). "Genomic transcriptional response to loss of chromosomal supercoiling in Escherichia coli." Genome Biol 5(11);R87. PMID: 15535863

Ruthenburg05: Ruthenburg AJ, Graybosch DM, Huetsch JC, Verdine GL (2005). "A superhelical spiral in the Escherichia coli DNA gyrase A C-terminal domain imparts unidirectional supercoiling bias." J Biol Chem 280(28);26177-84. PMID: 15897198

Schoeffler10: Schoeffler AJ, May AP, Berger JM (2010). "A domain insertion in Escherichia coli GyrB adopts a novel fold that plays a critical role in gyrase function." Nucleic Acids Res 38(21);7830-44. PMID: 20675723

Sissi05: Sissi C, Marangon E, Chemello A, Noble CG, Maxwell A, Palumbo M (2005). "The effects of metal ions on the structure and stability of the DNA gyrase B protein." J Mol Biol 353(5);1152-60. PMID: 16223508

Smelkova01: Smelkova N, Marians KJ (2001). "Timely release of both replication forks from oriC requires modulation of origin topology." J Biol Chem 276(42);39186-91. PMID: 11504719

Smith06a: Smith AB, Maxwell A (2006). "A strand-passage conformation of DNA gyrase is required to allow the bacterial toxin, CcdB, to access its binding site." Nucleic Acids Res 34(17);4667-76. PMID: 16963775

Staudenbauer81: Staudenbauer WL, Orr E (1981). "DNA gyrase: affinity chromatography on novobiocin-Sepharose and catalytic properties." Nucleic Acids Res 9(15);3589-603. PMID: 6269086

Steck84: Steck TR, Pruss GJ, Manes SH, Burg L, Drlica K (1984). "DNA supercoiling in gyrase mutants." J Bacteriol 158(2);397-403. PMID: 6327603

Sugino78: Sugino A, Higgins NP, Brown PO, Peebles CL, Cozzarelli NR (1978). "Energy coupling in DNA gyrase and the mechanism of action of novobiocin." Proc Natl Acad Sci U S A 75(10);4838-42. PMID: 368801

Sugino80: Sugino A, Higgins NP, Cozzarelli NR (1980). "DNA gyrase subunit stoichiometry and the covalent attachment of subunit A to DNA during DNA cleavage." Nucleic Acids Res 8(17);3865-74. PMID: 6255421

Sugino80a: Sugino A, Cozzarelli NR (1980). "The intrinsic ATPase of DNA gyrase." J Biol Chem 255(13);6299-306. PMID: 6248518

Thornton94: Thornton M, Armitage M, Maxwell A, Dosanjh B, Howells AJ, Norris V, Sigee DC (1994). "Immunogold localization of GyrA and GyrB proteins in Escherichia coli." Microbiology 140 ( Pt 9);2371-82. PMID: 7952188

Tsai97: Tsai FT, Singh OM, Skarzynski T, Wonacott AJ, Weston S, Tucker A, Pauptit RA, Breeze AL, Poyser JP, O'Brien R, Ladbury JE, Wigley DB (1997). "The high-resolution crystal structure of a 24-kDa gyrase B fragment from E. coli complexed with one of the most potent coumarin inhibitors, clorobiocin." Proteins 28(1);41-52. PMID: 9144789

UniProt15: UniProt Consortium (2015). "UniProt version 2015-08 released on 2015-07-22." 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."

Wigley91: Wigley DB, Davies GJ, Dodson EJ, Maxwell A, Dodson G (1991). "Crystal structure of an N-terminal fragment of the DNA gyrase B protein." Nature 351(6328);624-9. PMID: 1646964

Williams01: Williams NL, Howells AJ, Maxwell A (2001). "Locking the ATP-operated clamp of DNA gyrase: probing the mechanism of strand passage." J Mol Biol 306(5);969-84. PMID: 11237612

Williams99: Williams NL, Maxwell A (1999). "Probing the two-gate mechanism of DNA gyrase using cysteine cross-linking." Biochemistry 38(41);13502-11. PMID: 10521257

Yang88a: Yang Y, Ames GF (1988). "DNA gyrase binds to the family of prokaryotic repetitive extragenic palindromic sequences." Proc Natl Acad Sci U S A 85(23);8850-4. PMID: 2848243

Other References Related to Gene Regulation

Cameron11: Cameron AD, Stoebel DM, Dorman CJ (2011). "DNA supercoiling is differentially regulated by environmental factors and FIS in Escherichia coli and Salmonella enterica." Mol Microbiol. PMID: 21276095

Menzel87: Menzel R, Gellert M (1987). "Modulation of transcription by DNA supercoiling: a deletion analysis of the Escherichia coli gyrA and gyrB promoters." Proc Natl Acad Sci U S A 84(12);4185-9. PMID: 3035573

Schneider99: Schneider R, Travers A, Kutateladze T, Muskhelishvili G (1999). "A DNA architectural protein couples cellular physiology and DNA topology in Escherichia coli." Mol Microbiol 34(5);953-64. PMID: 10594821

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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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