Systematic Structure-Activity Analysis of Microcin J25
نویسندگان
چکیده
منابع مشابه
Antibacterial activity evaluation of microcin J25 against diarrheagenic Escherichia coli.
The inhibitory activities of known microcins were evaluated against some diarrheagenic Escherichia coli strains. Some antibacterial properties of microcin J25, the most active one, were studied. A rapid two-step purification was performed. The MIC and the minimum bactericidal concentration of J25 against E. coli O157:H7 were 1 and 100 microg ml(-1), respectively. A 10(4)-CFU ml(-1) contaminatio...
متن کاملAntibacterial Activity of the Peptide Microcin J25 Produced by Escherichia coli
Background and objectives: Bacteriocins are generally active antimicrobial peptides effective against bacteria closely related to the producer. Escherichia coli produce two bacteriocins: colicins and microcins. Microcin J25 (Mcc J25) is an antibacterial peptide that inhibits bacterial transcription by disrupting the nucleotide-uptake channel of bacterial RNA polymerase. The objective of this st...
متن کاملGrowth-phase-dependent expression of the cyclopeptide antibiotic microcin J25.
Microcin J25 is a 2,107-Da, plasmid-encoded, cyclopeptide antibiotic produced by Escherichia coli. We have isolated lacZ fusions to mcjA (encoding the 58-amino-acid microcin precursor) and mcjB and mcjC (which are required for microcin maturation), and the regulation of these fusions was used to identify factors that control the expression of these genes. The mcjA gene was found to be dramatica...
متن کاملComputational design of the lasso peptide antibiotic microcin J25.
Microcin J25 (MccJ25) is a 21 amino acid (aa) ribosomally synthesized antimicrobial peptide with an unusual structure in which the eight N-terminal residues form a covalently cyclized macrolactam ring through which the remaining 13 aa tail is fed. An open question is the extent of sequence space that can occupy such an extraordinary, highly constrained peptide fold. To begin answering this ques...
متن کاملStructure of microcin J25, a peptide inhibitor of bacterial RNA polymerase, is a lassoed tail.
Microcin J25 (MccJ25) is a 21-amino acid peptide inhibitor active against the DNA-dependent RNA polymerase of Gram negative bacteria. Previously, the structure of MccJ25 was reported to be a head-to-tail circle, cyclo(-G(1)GAGHVPEYF(10)VGIGTPISFY(20)G-). On the basis of biochemical studies, mass spectrometry, and NMR, we show that this structure is incorrect, and that the peptide has an extraor...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2008
ISSN: 0021-9258
DOI: 10.1074/jbc.m803995200