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    gyrA DNA gyrase subunit A [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 946614, updated on 3-Dec-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Single-molecule dynamics of DNA gyrase in evolutionarily distant bacteria Mycobacterium tuberculosis and Escherichia coli.

    Single-molecule dynamics of DNA gyrase in evolutionarily distant bacteria Mycobacterium tuberculosis and Escherichia coli.
    Galvin CJ, Hobson M, Meng JX, Ierokomos A, Ivanov IE, Berger JM, Bryant Z., Free PMC Article

    06/1/2023
    Escherichia coli GyrA Tower Domain Interacts with QnrB1 Loop B and Plays an Important Role in QnrB1 Protection from Quinolone Inhibition.

    Escherichia coli GyrA Tower Domain Interacts with QnrB1 Loop B and Plays an Important Role in QnrB1 Protection from Quinolone Inhibition.
    Chen C, Wang Y, Nakaminami H, Kim ES, Jacoby GA, Hooper DC., Free PMC Article

    07/24/2021
    Our findings indicate that the catalytic cycle of E. coli gyrase operates at high thermodynamic efficiency, and that the stability of DNA wrapping by the CTD provides one limit to DNA supercoil introduction, beyond which strand passage competes with ATP-dependent supercoil relaxation

    Modulated control of DNA supercoiling balance by the DNA-wrapping domain of bacterial gyrase.
    Hobson MJ, Bryant Z, Berger JM., Free PMC Article

    03/21/2020
    Inhibition of the gyrA promoter by transcription-coupled DNA supercoiling in Escherichia coli has been demonstrated.

    Inhibition of the gyrA promoter by transcription-coupled DNA supercoiling in Escherichia coli.
    Dages S, Dages K, Zhi X, Leng F., Free PMC Article

    11/2/2019
    The gyrA mutations were identified in nucleotide positions 248, 255, 259, 260, 261, 273 and 300, and mutations at positions 248 and 259 resulting in amino acid changes at positions 83 and 87 were associated with quinolone resistance.

    CRISPR/Cas9/sgRNA-mediated targeted gene modification confirms the cause-effect relationship between gyrA mutation and quinolone resistance in Escherichia coli.
    Qiu H, Gong J, Butaye P, Lu G, Huang K, Zhu G, Zhang J, Hathcock T, Cheng D, Wang C.

    09/21/2019
    High frequency of aac(6')-Ib-cr gene associated with double mutations in gyrA and parC is related to fluoroquinolone resistance

    High frequency of aac(6')-Ib-cr gene associated with double mutations in gyrA and parC in Escherichia coli isolates from patients with urinary tract infections.
    Volcão LM, Lacava JP, Gewehr MF, Leal VL, Ramis IB, Ramos DF, Gonçalves CV, Possuelo LG, Minarini LAR, da Silva PEA, von Groll A.

    09/21/2019
    Measuring the dwell time of gyrase bound to DNA revealed that most gyrase remain immobile for approximately 2 s, whereas enzymes in the vicinity of the replisome had a approximately 8 s dwell time, suggesting that when an excessive (+) supercoiling is present due to the fast progression of the fork, gyrase performs multiple rounds of catalysis without dissociating from DNA.

    Single-molecule imaging of DNA gyrase activity in living Escherichia coli.
    Stracy M, Wollman AJM, Kaja E, Gapinski J, Lee JE, Leek VA, McKie SJ, Mitchenall LA, Maxwell A, Sherratt DJ, Leake MC, Zawadzki P., Free PMC Article

    08/31/2019
    analysis of gyrase mutations in E.coli that could be responsible for increased quinolone resistive mechanisms among enteric pathogens; docking studies revealed displacement of quinolone binding site in mutated protein complex which resulted in lower binding energy as compared to the normal one

    Analytical profiling of mutations in quinolone resistance determining region of gyrA gene among UPEC.
    Varughese LR, Rajpoot M, Goyal S, Mehra R, Chhokar V, Beniwal V., Free PMC Article

    02/3/2018
    The present study was undertaken to better understand the dynamic behavior of the gyrA in Enterotoxigenic Escherichia coli [ETEC] and to decipher the structural changes associated with mutations, Ser83Leu and Ser83Leu/Asp87Asn, leading to ciprofloxacin antibiotic resistance in ETEC gyrA.

    Travelers' Diarrhea-Associated Enterotoxigenic Escherichia coli gyrA Mutants and Quinolone Antibiotic Affinity: A Molecular Dynamics Simulation and Residue Interaction Network Analysis.
    Mehla K, Ramana J.

    09/30/2017
    Data indicate the existence of interactions between the fluoroquinolone C-7 ring and both GyrA and GyrB.

    Fluoroquinolone-gyrase-DNA complexes: two modes of drug binding.
    Mustaev A, Malik M, Zhao X, Kurepina N, Luan G, Oppegard LM, Hiasa H, Marks KR, Kerns RJ, Berger JM, Drlica K., Free PMC Article

    08/9/2014
    This new structure is entirely consistent with the mutations in GyrA that confer Simocyclinone D8 resistance.

    A new crystal structure of the bifunctional antibiotic simocyclinone D8 bound to DNA gyrase gives fresh insight into the mechanism of inhibition.
    Hearnshaw SJ, Edwards MJ, Stevenson CE, Lawson DM, Maxwell A., Free PMC Article

    07/5/2014
    The C-terminal part of McbA is crucial for DNA gyrase inhibition and antibiotic uptake.

    The C-terminal part of microcin B is crucial for DNA gyrase inhibition and antibiotic uptake by sensitive cells.
    Shkundina I, Serebryakova M, Severinov K., Free PMC Article

    05/24/2014
    fluoroquinolone resistance appeared to be a stepwise phenomenon, with MIC increasing as point mutations in gyrA increased, but high-level- and multidrug resistance associated with fluoroquinolone resistance reflected overexpression of AcrAB efflux pump

    Evaluation of the contribution of gyrA mutation and efflux pumps to fluoroquinolone and multidrug resistance in pathogenic Escherichia coli isolates from dogs and cats.
    Shaheen BW, Boothe DM, Oyarzabal OA, Wang C, Johnson CM.

    03/26/2011
    acquisition of a fourth resistance mutation significantly increased fitness especially with the addition of a parC mutation (Topoisomerase IV) to a low-fitness strain carrying resistance mutations in gyrA (DNA Gyrase) and marR (drug efflux regulation)

    Interplay in the selection of fluoroquinolone resistance and bacterial fitness.
    Marcusson LL, Frimodt-Møller N, Hughes D., Free PMC Article

    01/21/2010
    Model analysis of experimental data indicates that bacterial toxin CcdB binding to DNA gyrase is an enthalpic process driven mainly by specific interactions between CcdB and the highly stable dimerization domain of the gyrase A subunit.

    Driving forces of gyrase recognition by the addiction toxin CcdB.
    Simic M, De Jonge N, Loris R, Vesnaver G, Lah J., Free PMC Article

    01/21/2010
    N-terminus verified by Edman degradation on mature peptide

    Fusions of the Escherichia coli gyrA and gyrB control regions to the galactokinase gene are inducible by coumermycin treatment.
    Menzel R, Gellert M., Free PMC Article

    11/5/2007
    binds to plasmid-encoded quinolone resistance protein Qnr

    Interaction of the plasmid-encoded quinolone resistance protein Qnr with Escherichia coli DNA gyrase.
    Tran JH, Jacoby GA, Hooper DC., Free PMC Article

    01/21/2010
    The low-resolution structure of the full-length A subunit (GyrA)was reported.

    Small-angle X-ray scattering reveals the solution structure of the full-length DNA gyrase a subunit.
    Costenaro L, Grossmann JG, Ebel C, Maxwell A.

    01/21/2010
    Analysis of DNA supercoiling by the E. coli GyrA C-terminal domain

    A superhelical spiral in the Escherichia coli DNA gyrase A C-terminal domain imparts unidirectional supercoiling bias.
    Ruthenburg AJ, Graybosch DM, Huetsch JC, Verdine GL.

    01/21/2010
    Crystallization of CcdB in complex with a GyrA fragment

    Crystallization of CcdB in complex with a GyrA fragment.
    Dao-Thi MH, Van Melderen L, De Genst E, Buts L, Ranquin A, Wyns L, Loris R.

    01/21/2010
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