Synthesis of the DNA Gyrase Inhibitor Microcin B17, a 43-Peptide Antibiotic with Eight Aromatic Heterocycles in its Backbone

1996 ◽  
Vol 35 (1314) ◽  
pp. 1506-1508 ◽  
Author(s):  
Georgi Videnov ◽  
Dietmar Kaiser ◽  
Marc Brooks ◽  
Günther Jung
Keyword(s):  
Dna Gyrase ◽  
Peptide Antibiotic ◽  
Aromatic Heterocycles ◽  
Microcin B17

scholarly journals The peptide antibiotic microcin B17 induces double-strand cleavage of DNA mediated by E. coli DNA gyrase.

1991 ◽  
Vol 10 (2) ◽  
pp. 467-476 ◽  
Author(s):  
J. L. Vizán ◽  
C. Hernández-Chico ◽  
I. del Castillo ◽  
F. Moreno
Keyword(s):  
Dna Gyrase ◽  
Peptide Antibiotic ◽  
E Coli ◽  
Microcin B17

scholarly journals Construction and Characterization of Mutations at Codon 751 of the Escherichia coli gyrB Gene That Confer Resistance to the Antimicrobial Peptide Microcin B17 and Alter the Activity of DNA Gyrase

2001 ◽  
Vol 183 (6) ◽  
pp. 2137-2140 ◽  
Author(s):  
Francisco J. del Castillo ◽  
Ignacio del Castillo ◽  
Felipe Moreno
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Dna Gyrase ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Peptide Antibiotic ◽  
Resistant Mutants ◽  
Different Levels ◽  
Microcin B17

ABSTRACT Microcin B17 is a peptide antibiotic that inhibits DNA replication in Escherichia coli by targeting DNA gyrase. Previously, two independently isolated microcin B17-resistant mutants were shown to harbor the same gyrB point mutation that results in the replacement of tryptophan 751 by arginine in the GyrB polypeptide. We used site-directed mutagenesis to construct mutants in which tryptophan 751 was deleted or replaced by other amino acids. These mutants exhibit altered DNA gyrase activity and different levels of resistance to microcin B17.

scholarly journals In vitro characterization of DNA gyrase inhibition by microcin B17 analogs with altered bisheterocyclic sites

2001 ◽  
Vol 98 (14) ◽  
pp. 7712-7717 ◽  
Author(s):  
D. B. Zamble ◽  
D. A. Miller ◽  
J. G. Heddle ◽  
A. Maxwell ◽  
C. T. Walsh ◽  
...  
Keyword(s):  
Dna Gyrase ◽  
In Vitro Characterization ◽  
Microcin B17

scholarly journals Architecture of Microcin B17 Synthetase: An Octameric Protein Complex Converting a Ribosomally Synthesized Peptide into a DNA Gyrase Poison

2019 ◽  
Vol 73 (4) ◽  
pp. 749-762.e5 ◽  
Author(s):  
Dmitry Ghilarov ◽  
Clare E.M. Stevenson ◽  
Dmitrii Y. Travin ◽  
Julia Piskunova ◽  
Marina Serebryakova ◽  
...  
Keyword(s):  
Protein Complex ◽  
Dna Gyrase ◽  
Microcin B17

scholarly journals The Highly Conserved TldD and TldE Proteins of Escherichia coli Are Involved in Microcin B17 Processing and in CcdA Degradation

2002 ◽  
Vol 184 (12) ◽  
pp. 3224-3231 ◽  
Author(s):  
Noureddine Allali ◽  
Hassan Afif ◽  
Martine Couturier ◽  
Laurence Van Melderen
Keyword(s):  
Escherichia Coli ◽  
Topoisomerase Ii ◽  
Resistance Mechanism ◽  
Physiological Role ◽  
Leader Peptide ◽  
Peptide Antibiotic ◽  
Amino Terminal ◽  
Bacterial Mutants ◽  
Microcin B17

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 encoded by the ccd poison-antidote system of plasmid F. This led to the idea that TldD and TldE could regulate gyrase function. We present in vivo evidence supporting the hypothesis that TldD and TldE have proteolytic activity. We show that in bacterial mutants devoid of either TldD or TldE activity, the MccB17 precursor accumulates and is not exported. Similarly, in the ccd system, we found that TldD and TldE are involved in CcdA and CcdA41 antidote degradation rather than being involved in the CcdB resistance mechanism. Interestingly, sequence database comparisons revealed that these two proteins have homologues in eubacteria and archaebacteria, suggesting a broader physiological role.

scholarly journals Posttranslational modifications in microcin B17 define an additional class of DNA gyrase inhibitor.

1994 ◽  
Vol 91 (10) ◽  
pp. 4519-4523 ◽  
Author(s):  
P. Yorgey ◽  
J. Lee ◽  
J. Kordel ◽  
E. Vivas ◽  
P. Warner ◽  
...  
Keyword(s):  
Posttranslational Modifications ◽  
Dna Gyrase ◽  
Microcin B17

ATP/GTP Hydrolysis Is Required for Oxazole and Thiazole Biosynthesis in the Peptide Antibiotic Microcin B17†

Biochemistry ◽  
1998 ◽  
Vol 37 (38) ◽  
pp. 13250-13261 ◽  
Author(s):  
Jill C. Milne ◽  
Andrew C. Eliot ◽  
Neil L. Kelleher ◽  
Christopher T. Walsh
Keyword(s):  
Peptide Antibiotic ◽  
Gtp Hydrolysis ◽  
Microcin B17

scholarly journals Protective Effect of Qnr on Agents Other than Quinolones That Target DNA Gyrase

2015 ◽  
Vol 59 (11) ◽  
pp. 6689-6695 ◽  
Author(s):  
George A. Jacoby ◽  
Marian A. Corcoran ◽  
David C. Hooper
Keyword(s):  
Protective Effect ◽  
Dna Gyrase ◽  
Molecular Probes ◽  
Protective Activity ◽  
Topoisomerase Iv ◽  
Synthetic Compounds ◽  
Target Dna ◽  
Simocyclinone D8 ◽  
Microcin B17 ◽  
Insight Into

ABSTRACTQnr is a plasmid-encoded and chromosomally determined protein that protects DNA gyrase and topoisomerase IV from inhibition by quinolones. Despite its prevalence worldwide and existence prior to the discovery of quinolones, its native function is not known. Other synthetic compounds and natural products also target bacterial topoisomerases. A number were studied as molecular probes to gain insight into how Qnr acts. Qnr blocked inhibition by synthetic compounds with somewhat quinolone-like structure that target the GyrA subunit, such as the 2-pyridone ABT-719, the quinazoline-2,4-dione PD 0305970, and the spiropyrimidinetrione pyrazinyl-alkynyl-tetrahydroquinoline (PAT), indicating that Qnr is not strictly quinolone specific, but Qnr did not protect against GyrA-targeting simocyclinone D8 despite evidence that both simocyclinone D8 and Qnr affect DNA binding to gyrase. Qnr did not affect the activity of tricyclic pyrimidoindole or pyrazolopyridones, synthetic inhibitors of the GyrB subunit, or nonsynthetic GyrB inhibitors, such as coumermycin A1, novobiocin, gyramide A, or microcin B17.Thus, in this set of compounds the protective activity of Qnr was confined to those that, like quinolones, trap gyrase on DNA in cleaved complexes.

Uptake and Mode of Action of the Peptide Antibiotic Microcin B17

1992 ◽  
pp. 15-17
Author(s):  
C. Hernández-Chico ◽  
O. Mayo ◽  
J. L. Vizán ◽  
M. Laviña ◽  
F. Moreno
Keyword(s):  
Mode Of Action ◽  
Peptide Antibiotic ◽  
Microcin B17
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