Disease relevance of sbmC

• Its NH2-terminal amino acid sequence of 16 residues was determined to be identical to that of a putative gene product (a polypeptide of 157 amino acids) encoded by yeeB (EMBL accession no. U00009) and sbmC (Baquero, M. R., Bouzon, M., Varea, J., and Moreno, F. (1995) Mol. Microbiol. 18, 301-311) of E. coli [1].
• Cyclothialidine is a new, potent DNA gyrase inhibitor isolated from Streptomyces filipinensis [2].
• Bacteriophage lambda promoters pL and pR: sequence determinants of in vivo activity and of sensitivity to the DNA gyrase inhibitor, coumermycin [3].
• Cells of Clostridium acetobutylicum treated with novoblocin, a DNA gyrase inhibitor, produced higher butyrate levels and lower solvent levels with acetone being the most affected [4].

High impact information on sbmC

• We have characterized regulation of a complex Chlamydomonas reinhardtii chloroplast (PA) whose activity is stimulated by the DNA gyrase inhibitor novobiocin, both in the alga itself and in a heterologous Escherichia coli plasmid system [5].
• Similar relaxation occurs when cells are treated with the DNA gyrase inhibitor coumermycin [6].
• Posttranslational modifications in microcin B17 define an additional class of DNA gyrase inhibitor [7].
• Previous studies have shown that GyrI, a regulatory factor of DNA gyrase activity, inhibits the supercoiling activity of DNA gyrase and that both overexpression and antisense expression of the gyrI gene suppress cell proliferation [8].
• Glutamate racemase is an endogenous DNA gyrase inhibitor [9].

Chemical compound and disease context of sbmC

• Escherichia coli cells resistant to the DNA gyrase inhibitor, ciprofloxacin, overproduce a 60 kD protein homologous to GroEL [10].

Biological context of sbmC

• sbmC, a stationary-phase induced SOS Escherichia coli gene, whose product protects cells from the DNA replication inhibitor microcin B17 [11].
• The region seems to contain four core binding sites (designated sbmA, sbmB, sbmC, and sbmD), each consisting of a similar number of nucleotides and including a homologous 15-bp sequence [12].
• In the present work, we have investigated the regulation of sbmC expression during SOS induction and the stationary growth phase using a single-copy sbmC'-'lacZ fusion [13].
• These findings demonstrate that H-NS regulates the sbmC expression via H-NS's direct binding to the promoter region [13].
• The gyrI (also called sbmC) gene product inhibits DNA gyrase activity in vitro, while the rob protein appears to function in transcriptional activation of efflux pumps [14].

Associations of sbmC with chemical compounds

• Both transcriptional fusions were induced during continuous growth at high temperature and their expression was reduced in cells grown in the presence of osmoprotectants (ectoine or glycine betaine) or the DNA gyrase inhibitor nalidixic acid [15].
• This topoisomerase was insensitive to the DNA gyrase inhibitor norfloxacin and unaffected by antibody directed against topoisomerase I. Relaxation of a unique plasmid topoisomer revealed that this decatenase changed the linking number of the DNA in steps of one and was therefore a type 1 topoisomerase [16].
• Novobiocin, a DNA gyrase inhibitor, strongly inhibits P4 DNA synthesis, indicating that form I DNA is the required substrate [17].
• Mechanism of inhibition of DNA gyrase by cyclothialidine, a novel DNA gyrase inhibitor [18].
• Compound 1 was found to be a DNA gyrase inhibitor having potency similar to ofloxacin but less than ciprofloxacin [19].

Other interactions of sbmC

• The gene is located at min 44 of the E. coli genetic map, close to the sbcB gene. sbmC expression is induced by DNA-damaging agents and, also, by the entry of cells into the stationary growth phase [11].
• Mutation in rpoS or hns causes the repression of the sbmC gene during the stationary growth phase [13].
• A mukB null mutant is hypersensitive to the DNA gyrase inhibitor novobiocin [20].

Analytical, diagnostic and therapeutic context of sbmC

• Assuming the identity of the gene (gyrI) encoding GyrI with the previously reported genes yeeB and sbmC, we cloned the gene after amplification by polymerase chain reaction and purified the 18-kDa protein from an E. coli strain overexpressing it [1].
• The gel mobility shift assay showed that purified H-NS protein directly bound with a high affinity to a DNA fragment carrying the sbmC promoter region [13].

References