The Periplasmic Protein MppA Requires an Additional Mutated Locus To Repress marA Expression in Escherichia coli
AUTOR(ES)
Bina, Xiaowen
FONTE
American Society for Microbiology
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=142866Documentos Relacionados
- The Periplasmic Murein Peptide-Binding Protein MppA Is a Negative Regulator of Multiple Antibiotic Resistance in Escherichia coli
- marA locus causes decreased expression of OmpF porin in multiple-antibiotic-resistant (Mar) mutants of Escherichia coli.
- Multidrug Resistance following Expression of the Escherichia coli marA Gene in Mycobacterium smegmatis
- marA, a regulated locus which controls expression of chromosomal multiple antibiotic resistance in Escherichia coli.
- Differential Expression of over 60 Chromosomal Genes in Escherichia coli by Constitutive Expression of MarA
