scholarly journals Transcriptional activation of promoters of the superoxide and multiple antibiotic resistance regulons by Rob, a binding protein of the Escherichia coli origin of chromosomal replication.

1996 ◽  
Vol 178 (9) ◽  
pp. 2507-2513 ◽  
Author(s):  
K W Jair ◽  
X Yu ◽  
K Skarstad ◽  
B Thöny ◽  
N Fujita ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Antibiotic Resistance ◽  
Transcriptional Activation ◽  
Binding Protein ◽  
Multiple Antibiotic Resistance ◽  
Chromosomal Replication

scholarly journals The Periplasmic Protein MppA Requires an Additional Mutated Locus To Repress marA Expression in Escherichia coli

2003 ◽  
Vol 185 (4) ◽  
pp. 1465-1469 ◽  
Author(s):  
Xiaowen Bina ◽  
Vincent Perreten ◽  
Stuart B. Levy
Keyword(s):  
Escherichia Coli ◽  
Antibiotic Resistance ◽  
Antibiotic Susceptibility ◽  
Type Strain ◽  
Wild Type Strain ◽  
Binding Protein ◽  
Periplasmic Protein ◽  
Multiple Antibiotic Resistance ◽  
Wild Type ◽  
Expression In Escherichia Coli

ABSTRACT Escherichia coli strain TP985, which has an insertional mutation in the gene for the periplasmic murein tripeptide binding protein MppA, was previously reported to overproduce MarA and exhibit a multiple-antibiotic resistance (Mar) phenotype (H. Li and J. T. Park, J. Bacteriol. 181:4842-4847, 1999). We found that TP985 contained a previously unrecognized marR mutation which was responsible for the Mar phenotype. Transduction of the mppA mutation from TP985 to another wild-type strain did not affect antibiotic susceptibility. Overproduction of MppA repressed marA transcription in TP985 but not in other mppA or marR mutants. Therefore, TP985 contains an additional unknown mutation(s) that facilitates the repression of marA expression by MppA.

scholarly journals The Periplasmic Murein Peptide-Binding Protein MppA Is a Negative Regulator of Multiple Antibiotic Resistance in Escherichia coli

1999 ◽  
Vol 181 (16) ◽  
pp. 4842-4847 ◽  
Author(s):  
HongShan Li ◽  
James T. Park
Keyword(s):  
Escherichia Coli ◽  
Antibiotic Resistance ◽  
Binding Protein ◽  
Wide Spectrum ◽  
Negative Regulator ◽  
Null Mutant ◽  
Multiple Antibiotic Resistance ◽  
Resistance Phenotype ◽  
E Coli ◽  
K 12

ABSTRACT MppA is a periplasmic binding protein in Escherichia coli essential for uptake of the cell wall murein tripeptidel-alanyl-γ-d-glutamyl-meso-diaminopimelate. We have found serendipitously that E. coli K-12 strains carrying a null mutation in mppA exhibit increased resistance to a wide spectrum of antibiotics and to cyclohexane. Normal sensitivity of the mppA mutant to these agents is restored by mppA expressed from a plasmid. As is observed in the multiple antibiotic resistance phenotype in E. coli cells, the mppA null mutant overproduces the transcriptional activator, MarA, resulting in expression of the membrane-bound AcrAB proteins that function as a drug efflux pump. Reduced production of OmpF similar to that observed in the multiple antibiotic resistance phenotype is also seen in the mppA mutant. These and other data reported herein indicate that MppA functions upstream of MarA in a signal transduction pathway to negatively regulate the expression ofmarA and hence of the MarA-driven multiple antibiotic resistance. Overproduction of cytoplasmic GadA and GadB and of several unidentified cytoplasmic membrane proteins as well as reduction in the amount of the outer membrane protein, OmpP, in the mppAnull mutant indicate that MppA regulates a number of genes in addition to those already known to be controlled by MarA.

scholarly journals Involvement of the Escherichia coli folate-binding protein YgfZ in RNA modification and regulation of chromosomal replication initiation

2006 ◽  
Vol 59 (1) ◽  
pp. 265-275 ◽  
Author(s):  
Tomotake Ote ◽  
Masayuki Hashimoto ◽  
Yoshiho Ikeuchi ◽  
Masayuki Su'etsugu ◽  
Tsutomu Suzuki ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Replication Initiation ◽  
Rna Modification ◽  
Chromosomal Replication ◽  
Folate Binding Protein

scholarly journals Inhibition of the multiple antibiotic resistance (mar) operon in Escherichia coli by antisense DNA analogs.

1997 ◽  
Vol 41 (12) ◽  
pp. 2699-2704 ◽  
Author(s):  
D G White ◽  
K Maneewannakul ◽  
E von Hofe ◽  
M Zillman ◽  
W Eisenberg ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Antibiotic Resistance ◽  
Antisense Oligonucleotides ◽  
Multiple Antibiotic Resistance ◽  
Wild Type ◽  
Lacz Expression ◽  
E Coli ◽  
Plasmid Construct ◽  
Dna Analogs ◽  
Susceptibility And Resistance

The multiple antibiotic resistance operon (marORAB) in Escherichia coli controls intrinsic susceptibility and resistance to multiple, structurally different antibiotics and other noxious agents. A plasmid construct with marA cloned in the antisense direction reduced LacZ expression from a constitutively expressed marA::lacZ translational fusion and inhibited the induced expression of LacZ in cells bearing the wild-type repressed fusion. The marA antisense construction also decreased the multiple antibiotic resistance of a Mar mutant. Two antisense phosphorothioate oligonucleotides, one targeted to marO and the other targeted to marA of the mar operon, introduced by heat shock or electroporation reduced LacZ expression in the strain having the marA::lacZ fusion. One antisense oligonucleotide, tested against a Mar mutant of E. coli ML308-225, increased the bactericidal activity of norfloxacin. These studies demonstrate the efficacy of exogenously delivered antisense oligonucleotides targeted to the marRAB operon in inhibiting expression of this chromosomal regulatory locus.

The association of acetylacetate (Acr AB-Tol C) and QepA genes with multiple antibiotic resistance among Escherichia coli clinical isolates

2019 ◽  
Vol 31 (3) ◽  
pp. 159-164
Author(s):  
Yaqdhan Alnomani ◽  
Abdolmajid Ghasemian ◽  
Mojtaba Memariani ◽  
Majid Eslami ◽  
Abdolreza Sabokrouh ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Antibiotic Resistance ◽  
Clinical Isolates ◽  
Multiple Antibiotic Resistance
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