1 take of microcin B17, microcin J25 (formerly
microcin 25), and bleomycin.
2 Microcins are a class of ribosomally synthesized antibac
3 While some
microcins are active as unmodified peptides, others are
4 lecular-weight post-translationally modified
microcins are produced by Escherichia coli, inferences b
5 Microcins are small secreted proteins that possess antim
6 Microcin B17 (MccB17) is a 3.1-kDa Escherichia coli anti
7 Microcin B17 (MccB17) is a peptidyl antibiotic that is s
8 Microcin B17 (MccB17) is a ribosomally encoded DNA-gyras
9 aturation of the Escherichia coli antibiotic
Microcin B17 (MccB17), the McbA prepro-antibiotic is mod
10 ta about three such microcins--microcin J25,
microcin B17 and microcin C7-C51--are discussed.
11 Microcin B17 has no detectable effect on gyrase-catalyse
12 Microcin B17 is a 3.1-kDa bactericidal peptide; the puta
13 Esherichia coli
microcin B17 is a posttranslationally modified peptide t
14 eavage produced by gyrase in the presence of
microcin B17 is different from that produced by quinolon
15 these motifs (D132, D147, and D199) reduced
Microcin B17 production in vivo and heterocycle formatio
16 gue 5'-adenylyl beta,gamma-imidodiphosphate,
microcin B17 stabilises a gyrase-dependent DNA cleavage
17 eterocycle formation, and an enzyme complex,
microcin B17 synthase, was purified and found to contain
18 ding and downstream heterocycle formation by
microcin B17 synthase.
19 The
microcin B17 synthetase converts glycine, serine, and cy
20 zoles and four oxazoles by the three subunit
Microcin B17 synthetase.
21 To produce the antibiotic
Microcin B17, four Cys and four Ser residues are convert
22 omycin, gramicidin S, rapamycin, indolmycin,
microcin B17, fumagillin, mycotoxins, Monascus pigments,
23 f BacA, SbmA, is implicated in the uptake of
microcin B17, microcin J25 (formerly microcin 25), and b
24 bmA mutants, namely, increased resistance to
microcin B17, microcin J25, and bleomycin, demonstrating
25 aturation of the Escherichia coli antibiotic
Microcin B17, the product of the mcbA gene is modified p
26 ght to protect DNA gyrase from the action of
microcin B17.
27 aturation of the Escherichia coli antibiotic
Microcin B17.
28 ro that confer antibiotic activity on mature
microcin B17.
29 nzymes involved in thiazole/oxazole-modified
microcin biosynthesis, a rapidly growing sector of natur
30 ng homology to genes of the Escherichia coli
Microcin C (McC) biosynthetic pathway.
31 Translation inhibitor
microcin C (McC) is a heptapeptide with an aspartate alp
32 Microcin C (McC) is a peptide-nucleotide antibiotic prod
33 Microcin C (McC) is a peptide-nucleotide antibiotic that
34 Microcin C (McC) is a potent antibacterial agent produce
35 Microcin C (McC) is heptapeptide adenylate antibiotic pr
36 Peptide-nucleotide antibiotic
microcin C (McC) is produced by some Escherichia coli st
37 Microcin C (McC), a peptide-nucleotide Trojan horse anti
38 Microcin C and related antibiotics are Trojan-horse pept
39 Recently, a
microcin C homologue from Bacillus amyloliquefaciens con
40 Microcin C is a heptapeptide-adenylate antibiotic produc
41 Here, we describe a novel
microcin C-like compound from Bacillus amyloliquefaciens
42 We show that
microcin C-like compounds carrying terminal cytosines ar
43 g sensitive cells in the same way as E. coli
microcin C.
44 The antibiotic
microcin C7 (McC) acts as a bacteriocide by inhibiting a
45 tyl tRNA synthetase "Trojan horse" inhibitor
microcin C7 (McC7) consists of a nonhydrolyzable asparty
46 oducer strains of Escherichia coli to afford
microcin C7 (MccC7), a "Trojan horse" antibiotic that co
47 MccA heptapeptide during the biosynthesis of
microcin C7 (MccC7), a 'Trojan horse' antibiotic.
48 ch microcins--microcin J25, microcin B17 and
microcin C7-C51--are discussed.
49 ng those that are structurally distinct from
microcin C7.
50 Moreover, we show that
microcins can act as narrow-spectrum therapeutics to inh
51 Microcin E492 (Mcc) is a pore-forming bacteriotoxin.
52 Microcin E492 (Mcc), a low molecular weight bacteriocin
53 chinery, to the C-terminal serine residue of
microcin E492 (MccE492), an 84 aa ribosomal antibiotic p
54 e remarkable post-translational tailoring of
microcin E492 (MccE492), an 84-residue protein toxin sec
55 The finding that
microcin E492 naturally exists both as functional toxic
56 We report here that
microcin E492, a peptide naturally produced by Klebsiell
57 Here we demonstrate that
microcins enable the probiotic bacterium Escherichia col
58 We suggest that
microcin exerts its effects through a mechanism that has
59 Low-molecular-weight
microcins from the post-translationally modified group t
60 sed on immunity to the antimicrobial peptide
microcin H47 (MccH47).
61 strate fragments of the structurally related
microcins H47, I47, and M.
62 ne-resistant mutants, are cross resistant to
microcin-
induced DNA cleavage.
63 is implicated in the uptake of microcin B17,
microcin J25 (formerly microcin 25), and bleomycin.
64 Peptide
microcin J25 (MccJ25) inhibits bacterial RNA polymerase.
65 The antibacterial peptide
microcin J25 (MccJ25) inhibits transcription by bacteria
66 21 amino acid peptide
Microcin J25 (MccJ25) inhibits transcription by bacteria
67 Microcin J25 (MccJ25) is a 21-amino acid peptide inhibit
68 Microcin J25 (MccJ25) is a 21-residue plasmid-encoded ri
69 Microcin J25 (MccJ25) is a ribosomally synthesized antim
70 Microcin J25 (MccJ25) is an antimicrobial peptide with a
71 The antimicrobial peptide
microcin J25 (MccJ25) is matured by two enzymes, McjB an
72 Mutagenesis of the lasso peptide
microcin J25 (MccJ25) with two cysteine residues followe
73 to make Escherichia coli cells resistant to
microcin J25 (MccJ25), a bactericidal 21-amino acid pept
74 tructure of capistruin is similar to that of
microcin J25 (MccJ25), a threaded-lasso antibacterial pe
75 amely, increased resistance to microcin B17,
microcin J25, and bleomycin, demonstrating the functiona
76 functional data about three such microcins--
microcin J25, microcin B17 and microcin C7-C51--are disc
77 chemical syntheses of the cyclic antibiotic
microcin J25, the 56-amino acid streptococcal protein G
78 press and secrete the antimicrobial peptide,
Microcin J25.
79 Our work provides the first evidence that
microcins mediate inter- and intraspecies competition am
80 uctural and functional data about three such
microcins--
microcin J25, microcin B17 and microcin C7-C5
81 Microcin PDI inhibits a diversity of pathogenic Escheric
82 Microcin-
producing EcN limits the growth of competitors
83 therapeutic administration of the wild-type,
microcin-
producing EcN to mice previously infected with
84 regulation of iron acquisition, capsule, and
microcin secretion genes, thus partially mimicking growt
85 lysaccharide synthesis, drug resistance, and
microcin secretion.
86 dified posttranslationally by the multimeric
Microcin synthetase complex (composed of McbB, C, and D)
87 ified post-translationally by the multimeric
microcin synthetase complex (composed of the McbB, -C, a
88 the overexpression and rapid purification of
microcin synthetase has been developed using a calmoduli
89 k indicate that MccPDI is unique amongst the
microcins that have been described to date.
90 e repurposing of a thiazole/oxazole-modified
microcin (
TOMM) cyclodehydratase to site-specifically in
91 Thiazole/oxazole-modified
microcins (
TOMMs) are a class of post-translationally mo
92 The thiazole/oxazole-modified
microcins (
TOMMs) represent a burgeoning class of riboso
93 novel siderophore receptors), cvaC (colicin [
microcin]
V), traT (serum-resistance associated), ibeA (
94 th antibiotic biosynthesis in vivo, yielding
microcin with six, seven, and eight rings, all with bioa