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Relevant bibliographies by topics / E. coli CcdB

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Journal articles

Academic literature on the topic 'E. coli CcdB'

Author: Grafiati

Published: 6 September 2023

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Journal articles on the topic "E. coli CcdB"

1

Wang, Hailong, Xiaoying Bian, Liqiu Xia, et al. "Improved seamless mutagenesis by recombineering using ccdB for counterselection." Nucleic Acids Research 42, no. 5 (2013): e37-e37. http://dx.doi.org/10.1093/nar/gkt1339.

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Abstract Recombineering, which is the use of homologous recombination for DNA engineering in Escherichia coli, usually uses antibiotic selection to identify the intended recombinant. When combined in a second step with counterselection using a small molecule toxin, seamless products can be obtained. Here, we report the advantages of a genetic strategy using CcdB as the counterselectable agent. Expression of CcdB is toxic to E. coli in the absence of the CcdA antidote so counterselection is initiated by the removal of CcdA expression. CcdB counterselection is robust and does not require titrati

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2

Allali, Noureddine, Hassan Afif, Martine Couturier, and Laurence Van Melderen. "The Highly Conserved TldD and TldE Proteins of Escherichia coli Are Involved in Microcin B17 Processing and in CcdA Degradation." Journal of Bacteriology 184, no. 12 (2002): 3224–31. http://dx.doi.org/10.1128/jb.184.12.3224-3231.2002.

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ABSTRACT Microcin B17 (MccB17) is a peptide antibiotic produced by Escherichia coli strains carrying the pMccB17 plasmid. MccB17 is synthesized as a precursor containing an amino-terminal leader peptide that is cleaved during maturation. Maturation requires the product of the chromosomal tldE (pmbA) gene. Mature microcin is exported across the cytoplasmic membrane by a dedicated ABC transporter. In sensitive cells, MccB17 targets the essential topoisomerase II DNA gyrase. Independently, tldE as well as tldD mutants were isolated as being resistant to CcdB, another natural poison of gyrase enco

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3

Aguirre-Ramírez, Marisela, Jesús Ramírez-Santos, Laurence Van Melderen, and M. Carmen Gómez-Eichelmann. "Expression of the F plasmid ccd toxin–antitoxin system in Escherichia coli cells under nutritional stress." Canadian Journal of Microbiology 52, no. 1 (2006): 24–30. http://dx.doi.org/10.1139/w05-107.

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The ccd system of the F plasmid encodes CcdB, a protein toxic to DNA-gyrase, and CcdA, its antitoxin. The function attributed to this system is to contribute to plasmid stability by killing bacteria that lose the plasmid during cell division. However, the function of ccd in resting bacteria is not clear. Results presented show that ccd transcription increases as bacteria enter stationary phase and that the amount of the Ccd proteins is higher in bacteria under nutritional stress than in growing bacteria. Moreover, an increase in the frequency of Lac+ "adaptive" mutations was observed in statio

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4

Zhang, Qing, Zhenya Yan, Yan Xu, Jian Sun, and Guangdong Shang. "Characterization of Inducible ccdB Gene as a Counterselectable Marker in Escherichia coli Recombineering." Current Microbiology 74, no. 8 (2017): 961–64. http://dx.doi.org/10.1007/s00284-017-1273-3.

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5

BAJAJ, Kanika, Ghadiyaram CHAKSHUSMATHI, Kiran BACHHAWAT-SIKDER, Avadhesha SUROLIA, and Raghavan VARADARAJAN. "Thermodynamic characterization of monomeric and dimeric forms of CcdB (controller of cell division or death B protein)." Biochemical Journal 380, no. 2 (2004): 409–17. http://dx.doi.org/10.1042/bj20031528.

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The protein CcdB (controller of cell division or death B) is an F-plasmid-encoded toxin that acts as an inhibitor of Escherichia coli DNA gyrase. The stability and aggregation state of CcdB have been characterized as a function of pH and temperature. Size-exclusion chromatography revealed that the protein is a dimer at pH 7.0, but a monomer at pH 4.0. CD analysis and fluorescence spectroscopy showed that the monomer is well folded, and has similar tertiary structure to the dimer. Hence intersubunit interactions are not required for folding of individual subunits. The stability of both forms wa

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6

Hashimi, Saeed M., Melisa K. Wall, Andrew B. Smith, Anthony Maxwell, and Robert G. Birch. "The Phytotoxin Albicidin is a Novel Inhibitor of DNA Gyrase." Antimicrobial Agents and Chemotherapy 51, no. 1 (2007): 181–87. http://dx.doi.org/10.1128/aac.00918-06.

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ABSTRACT Xanthomonas albilineans produces a family of polyketide-peptide compounds called albicidins which are highly potent antibiotics and phytotoxins as a result of their inhibition of prokaryotic DNA replication. Here we show that albicidin is a potent inhibitor of the supercoiling activity of bacterial and plant DNA gyrases, with 50% inhibitory concentrations (40 to 50 nM) less than those of most coumarins and quinolones. Albicidin blocks the religation of the cleaved DNA intermediate during the gyrase catalytic sequence and also inhibits the relaxation of supercoiled DNA by gyrase and to

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7

Loris, Remy, Minh-Hoa Dao-Thi, El Mustapha Bahassi, et al. "Crystal structure of CcdB, a topoisomerase poison from E. coli 1 1Edited by T. Richmond." Journal of Molecular Biology 285, no. 4 (1999): 1667–77. http://dx.doi.org/10.1006/jmbi.1998.2395.

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8

Maki, S., S. Takiguchi, T. Miki, and T. Horiuchi. "Modulation of DNA supercoiling activity of Escherichia coli DNA gyrase by F plasmid proteins. Antagonistic actions of LetA (CcdA) and LetD (CcdB) proteins." Journal of Biological Chemistry 267, no. 17 (1992): 12244–51. http://dx.doi.org/10.1016/s0021-9258(19)49831-1.

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9

Baishya, S., A. Das Talukdar, and M. Dutta Choudhury. "Secondary resistance gene ccdB and repA2 facilitates carbapenem resistance in Escherichia coli carrying New Delhi Metallo-beta-lactamase." International Journal of Infectious Diseases 101 (December 2020): 36–37. http://dx.doi.org/10.1016/j.ijid.2020.09.129.

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10

Sundararaj, S. "The CyberCell Database (CCDB): a comprehensive, self-updating, relational database to coordinate and facilitate in silico modeling of Escherichia coli." Nucleic Acids Research 32, no. 90001 (2004): 293D—295. http://dx.doi.org/10.1093/nar/gkh108.

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