نتایج جستجو برای: tolc

تعداد نتایج: 522  

2017
Razieh Pourahmad Jaktaji Farzaneh Zargampoor

AcrAB-TolC is a major efflux pump in Escherichia coli. It was reported that tolC is overexpressed and involves in improving the organic solvent tolerance level in Escherichia colimarR mutants that are resistant to several antibiotics, such as ciprofloxacin. Low and intermediate levels resistance did not improve organic solvent tolerance. Thus, it was decided to measure tolC expression and organ...

Journal: :International Journal of Molecular Sciences 2009
Nehaya Al-Karablieh Helge Weingart Matthias S. Ullrich

AcrAB-TolC is the major multidrug efflux system in Enterobacteriaceae recognizing structurally unrelated molecules including antibiotics, dyes, and detergents. Additionally, in Escherichia coli it mediates resistance to bile salts. In the plant pathogen Erwinia amylovora AcrAB-TolC is required for virulence and phytoalexin resistance. Exchange analysis of AcrAB-TolC was conducted by complementi...

Journal: :Journal of bacteriology 2004
Anne Marie Augustus Teresa Celaya Fasahath Husain Matthew Humbard Rajeev Misra

The TolC protein of Escherichia coli, through its interaction with AcrA and AcrB, is thought to form a continuous protein channel that expels inhibitors from the cell. Consequently, tolC null mutations display a hypersensitive phenotype. Here we report the isolation and characterization of tolC missense mutations that direct the synthesis of mutant TolC proteins partially disabled in their effl...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2011
Xue-Yuan Pei Philip Hinchliffe Martyn F Symmons Eva Koronakis Roland Benz Colin Hughes Vassilis Koronakis

In bacterial drug resistance and virulence pumps, an inner membrane (IM) transporter and periplasmic adaptor recruit an outer membrane (OM) trimeric TolC exit duct that projects an α-helical tunnel across the periplasm. The TolC periplasmic entrance is closed by densely packed α-helical coiled coils, inner H7/H8, and outer H3/H4, constrained by a hydrogen bond network. On recruitment, these coi...

AcrAB-TolC is a major efflux pump in Escherichia coli. It was reported that tolC is overexpressed and involves in improving the organic solvent tolerance level in Escherichia coli marR mutants that are resistant to several antibiotics, such as ciprofloxacin. Low and intermediate levels resistance did not improve organic solvent tolerance. Thus, in this descriptive-experimental study it was deci...

Journal: :Journal of bacteriology 1996
J A Fralick

A study examining the influence of TolC on AcrA, AcrR, and MarR1 mutants indicates that functional TolC is required for the operation of the AcrAB efflux system and for the expression of the Mar phenotype. That the effect of TolC on the AcrAB pump is not regulatory in nature is shown by studies measuring the influence of a tolC::Tn10 insertion mutation on the expression of an acrA::lacZ reporte...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2007
Sune Lobedanz Evert Bokma Martyn F Symmons Eva Koronakis Colin Hughes Vassilis Koronakis

Bacteria such as Escherichia coli and Pseudomonas aeruginosa expel antibiotics and other inhibitors via tripartite multidrug efflux pumps spanning the inner and outer membranes and the intervening periplasmic space. A key event in pump assembly is the recruitment of an outer membrane-anchored TolC exit duct by the adaptor protein of a cognate inner membrane translocase, establishing a contiguou...

2012
Minho Lee So-Young Jun Bo-Young Yoon Saemee Song Kangseok Lee Nam-Chul Ha

The Hly translocator complex of Escherichia coli catalyzes type I secretion of the toxin hemolysin A (HlyA). In this complex, HlyB is an inner membrane ABC (ATP Binding Cassette)-type transporter, TolC is an outer membrane channel protein, and HlyD is a periplasmic adaptor anchored in the inner membrane that bridges HlyB to TolC. This tripartite organization is reminiscent of that of drug efflu...

Journal: :Journal of bacteriology 1997
J Hwang X Zhong P C Tai

The antibacterial peptide toxin colicin V uses a dedicated signal sequence-independent system for its secretion in Escherichia coli and requires the products of three genes, cvaA, cvaB, and tolC. As a member of the membrane fusion protein family, CvaA is supposed to form a bridge that connects the inner and outer membranes via interaction with CvaB and TolC, respectively. In this study, we inve...

Journal: :Antimicrobial agents and chemotherapy 2010
Nazia Kamal William M Shafer

Neisseria meningitidis can produce a TolC-like protein needed for secretion of FrpC but not efflux of antimicrobials. We now report that expression of the meningococcal tolC gene in a TolC-deficient strain of Escherichia coli can restore properties of alpha-hemolysis and antimicrobial resistance known to involve efflux pumps.

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