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Characterization of AcrAB-TolC antib...

Husain, Fasahath.

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Characterization of AcrAB-TolC antibiotic efflux complex of Escherichia coli.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Characterization of AcrAB-TolC antibiotic efflux complex of Escherichia coli./
作者:	Husain, Fasahath.
面頁冊數:	164 p.
附註:	Adviser: Rajeev Misra.
Contained By:	Dissertation Abstracts International67-06B.
標題:	Biology, Genetics. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3220305
ISBN:	9780542741876

Characterization of AcrAB-TolC antibiotic efflux complex of Escherichia coli.
Husain, Fasahath.

Characterization of AcrAB-TolC antibiotic efflux complex of Escherichia coli. - 164 p.

Adviser: Rajeev Misra.

Thesis (Ph.D.)--Arizona State University, 2006.

Escherichia coli is a Gram-negative bacterium. It has a distinct inner membrane (cytoplasmic membrane) and an outer membrane, separated by a periplasm. The presence of outer membrane makes a Gram-negative organism impermeable to many antimicrobial compounds, conferring innate resistance. Like many other organisms, E. coli has an efflux system to pump out antimicrobials that enter the cell using a tripartite complex comprised of AcrA-AcrB-TolC proteins. ACrAB-TolC constitutes the major efflux system in E. coli. The efflux apparatus removes the antimicrobials out of the cytoplasm/inner membrane into the medium. AcrB is the energized component of the inner membrane that binds the substrate and pumps it out of the cell through the outer membrane component, TolC. AcrA has a large domain in the periplasm which is predicted to stabilize the AcrB-TolC complex. Each of these components is essential for efflux activity. In this study, TolC mutants that increase the outer membrane permeability have been characterized. This study gives an insight into the opening of the otherwise nearly closed TolC periplasmic aperture. Interactions of periplasmic component AcrA with the outer membrane component TolC has been shown biochemically through cross-linking studies. Finally, through genetic analysis functional interactions between the inner membrane component AcrB and the outer membrane component TolC have been revealed. This study suggests that AcrB is involved in the opening of the TolC's periplasmic aperture. There is also indirect evidence that AcrA could be involved in opening of TolC periplasmic aperture.

ISBN: 9780542741876Subjects--Topical Terms:

1017730
Biology, Genetics.

Characterization of AcrAB-TolC antibiotic efflux complex of Escherichia coli.
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520 $a Escherichia coli is a Gram-negative bacterium. It has a distinct inner membrane (cytoplasmic membrane) and an outer membrane, separated by a periplasm. The presence of outer membrane makes a Gram-negative organism impermeable to many antimicrobial compounds, conferring innate resistance. Like many other organisms, E. coli has an efflux system to pump out antimicrobials that enter the cell using a tripartite complex comprised of AcrA-AcrB-TolC proteins. ACrAB-TolC constitutes the major efflux system in E. coli. The efflux apparatus removes the antimicrobials out of the cytoplasm/inner membrane into the medium. AcrB is the energized component of the inner membrane that binds the substrate and pumps it out of the cell through the outer membrane component, TolC. AcrA has a large domain in the periplasm which is predicted to stabilize the AcrB-TolC complex. Each of these components is essential for efflux activity. In this study, TolC mutants that increase the outer membrane permeability have been characterized. This study gives an insight into the opening of the otherwise nearly closed TolC periplasmic aperture. Interactions of periplasmic component AcrA with the outer membrane component TolC has been shown biochemically through cross-linking studies. Finally, through genetic analysis functional interactions between the inner membrane component AcrB and the outer membrane component TolC have been revealed. This study suggests that AcrB is involved in the opening of the TolC's periplasmic aperture. There is also indirect evidence that AcrA could be involved in opening of TolC periplasmic aperture.
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