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D0690

Sigma-Aldrich

DNA Gyrase from Escherichia coli

aqueous glycerol solution

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About This Item

Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

Escherichia coli

Quality Level

form

aqueous glycerol solution

mol wt

~374 kDa

concentration

≥2 unit/μL

technique(s)

cell based assay: suitable

UniProt accession no.

application(s)

cell analysis

shipped in

dry ice

storage temp.

−70°C

Gene Information

Escherichia coli K12 ... gyrA(946614) , gyrB(948211)

Application

DNA gyrase from Escherichia coli has been used in a study to investigate a comparative proteomic approach to better define Deinococcus nucleoid specificities. DNA gyrase from Escherichia coli has also been used in a study to investigate the role of the DnaK-ClpB bichaperone system in DNA gyrase reactivation.

Biochem/physiol Actions

DNA gyrase is supplied as an A2B2 holoenzyme. The molecular mass of subunit A is 97 kDa and that of subunit B is 90 kDa. It catalyzes the ATP-dependent introduction of negative supercoils into relaxed DNA. DNA gyrase has been successfully converted into a type II topoisomerase by mutagenesis experiments.
Can be used to supercoil plasmids.

Unit Definition

One unit of gyrase activity will supercoil 0.5 micrograms of pBR-322 DNA in 30 minutes at 37 °C.

Other Notes

Solution in 50% Glycerol containing Tris buffer, DTT and EDTA.

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Magali Toueille et al.
Journal of proteomics, 75(9), 2588-2600 (2012-03-27)
Compared to radiation-sensitive bacteria, the nucleoids of radiation-resistant Deinococcus species show a higher degree of compaction. Such a condensed nucleoid may contribute to the extreme radiation resistance of Deinococcus by limiting dispersion of radiation-induced DNA fragments. Architectural proteins may play
Teresa Lara-Ortíz et al.
Canadian journal of microbiology, 58(2), 195-199 (2012-01-24)
In Escherichia coli cells, an increase in temperature induces immediate DNA relaxation, followed by the fast recovery of DNA supercoiling. DNA gyrase, proteins synthesized during heat stress, and chaperone DnaK have been proposed to participate in this recovery. However, the
J C Wang
Annual review of biochemistry, 65, 635-692 (1996-01-01)
The various problems of disentangling DNA strands or duplexes in a cell are all rooted in the double-helical structure of DNA. Three distinct subfamilies of enzymes, known as the DNA topoisomerases, have evolved to solve these problems. This review focuses
S Lokeswara Balakrishna et al.
Archives of biochemistry and biophysics, 532(2), 91-102 (2013-02-13)
HIV-1 reverse transcription (RTn) involves synthesis of double strand DNA (dsDNA) from viral genomic RNA. Topoisomerase II (Topo II) alpha and beta maintains topological reorganization of dsDNA regions and catalytic inhibition of these isoforms repressed viral replicative cycle. Present study
David P Boyle et al.
Biochimica et biophysica acta, 1835(2), 230-242 (2013-02-14)
The analysis of clinical breast samples using biomarkers is integral to current breast cancer management. Currently, a limited number of targeted therapies are standard of care in breast cancer treatment. However, these targeted therapies are only suitable for a subset

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