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PMID: 8682804 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The activity of the high-affinity K+ uptake system Kdp sensitizes cells of Escherichia coli to methylglyoxal.

Journal of bacteriology ·Vol. 178 ·No. 13 ·1996-07-00 ·Pages 3957-61

Ferguson GP, Chacko AD, Lee CH, Booth IR, Lee C

Abstract

Expression of the Kdp system sensitizes cells to methylglyoxal (MG) whether this electrophile is added externally or is synthesized endogenously. The basis of this enhanced sensitivity is the maintenance of a higher cytoplasmic pH (pHi) in cells expressing Kdp. In such cells, MG elicits rapid cytoplasmic acidification via KefB and KefC, but the steady-state pHi attained is still too high to confer protection Lowering pHi further by incubation with acetate increases the sensitivity of cells to MG.

MeSH Terms
Adenosine Triphosphatases/metabolism Antiporters/metabolism Bacterial Proteins/metabolism Carrier Proteins/metabolism Cation Transport Proteins Escherichia coli/drug effects,growth & development,metabolism Escherichia coli Proteins Hydrogen-Ion Concentration Potassium/metabolism Potassium Channels/metabolism Potassium-Hydrogen Antiporters Pyruvaldehyde/pharmacology
Chemicals
Antiporters Bacterial Proteins Carrier Proteins Cation Transport Proteins Escherichia coli Proteins Potassium Channels Potassium-Hydrogen Antiporters KefC protein, E coli Pyruvaldehyde Adenosine Triphosphatases potassium translocating Kdp-ATPase, E coli Potassium
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Ferguson G P
Department of Molecular & Cell Biology, University of Aberdeen, United Kingdom.
Chacko A D
Lee C H
Booth I R
Lee C
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26 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1996-07-00
Pages
3957-61
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC232660
Subset
IM
Grants
Wellcome Trust · United Kingdom
Corrections
ErratumIn
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