PMID:21143325: Difference between revisions
New PMID: Page! |
imported>Wikientrybot change PMID template to TableEdit version |
||
| (2 intermediate revisions by 2 users not shown) | |||
| Line 1: | Line 1: | ||
{{RightTOC}} | |||
<!--box uid=d41d8cd98f00b204e9800998ecf8427e.181654.O4f91e60c79d43--> | |||
<!-- | |||
****************************************************************************************** | |||
* | |||
* ** PLEASE DON'T EDIT THIS TABLE DIRECTLY. Use the edit table link under the table. ** | |||
* | |||
****************************************************************************************** --> | |||
{| id="O4f91e60c79d43" class=" tableEdit PMID_info_table" | |||
|- | |||
!align=left |Citation | |||
|| | |||
'''Ozyamak, E, Black, SS, Walker, CA, Maclean, MJ, Bartlett, W, Miller, S and Booth, IR''' (2010) The critical role of S-lactoylglutathione formation during methylglyoxal detoxification in Escherichia coli. ''Mol. Microbiol.'' '''78''':1577-90 | |||
|- | |||
!align=left |Abstract | |||
|| | |||
Survival of exposure to methylglyoxal (MG) in Gram-negative pathogens is largely dependent upon the operation of the glutathione-dependent glyoxalase system, consisting of two enzymes, GlxI (gloA) and GlxII (gloB). In addition, the activation of the KefGB potassium efflux system is maintained closed by glutathione (GSH) and is activated by S-lactoylGSH (SLG), the intermediate formed by GlxI and destroyed by GlxII. Escherichia coli mutants lacking GlxI are known to be extremely sensitive to MG. In this study we demonstrate that a ΔgloB mutant is as tolerant of MG as the parent, despite having the same degree of inhibition of MG detoxification as a ΔgloA strain. Increased expression of GlxII from a multicopy plasmid sensitizes E. coli to MG. Measurement of SLG pools, KefGB activity and cytoplasmic pH shows these parameters to be linked and to be very sensitive to changes in the activity of GlxI and GlxII. The SLG pool determines the activity of KefGB and the degree of acidification of the cytoplasm, which is a major determinant of the sensitivity to electrophiles. The data are discussed in terms of how cell fate is determined by the relative abundance of the enzymes and KefGB. | |||
|- | |||
!align=left |Links | |||
|| | |||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=21143325 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3412212 PMC3412212] | |||
Online version:[http://dx.doi.org/10.1111/j.1365-2958.2010.07426.x 10.1111/j.1365-2958.2010.07426.x] | |||
|- | |||
!align=left |Keywords | |||
|| | |||
Escherichia coli/drug effects; Escherichia coli/enzymology; Escherichia coli/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Glutathione/analogs & derivatives; Glutathione/metabolism; Lactoylglutathione Lyase/genetics; Lactoylglutathione Lyase/metabolism; Microbial Viability; Potassium-Hydrogen Antiporters/genetics; Potassium-Hydrogen Antiporters/metabolism; Pyruvaldehyde/metabolism; Pyruvaldehyde/pharmacology | |||
|- class="tableEdit_footer" | |||
|<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.181654.O4f91e60c79d43&page=181654&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> || | |||
|} | |||
<!--box uid=d41d8cd98f00b204e9800998ecf8427e.181654.O4f91e60c79d43--> | |||
==Significance {{HelpIcon|Help:Literature}} == | |||
{{LitSignificance}} | |||
== Useful Materials and Methods {{HelpIcon|Help:Literature}}== | |||
{{LitMaterials}} | |||
==Annotations {{HelpIcon|Help:Literature}}== | |||
<protect><annotationlinks/></protect> | |||
==EcoliWiki Links {{HelpIcon|Help:Literature}} == | |||
{{LitLinks}} | |||
==See also== | |||
==References== | |||
{{RefHelp}} | |||
<references/> | |||
Latest revision as of 04:37, 15 September 2013
| Citation |
Ozyamak, E, Black, SS, Walker, CA, Maclean, MJ, Bartlett, W, Miller, S and Booth, IR (2010) The critical role of S-lactoylglutathione formation during methylglyoxal detoxification in Escherichia coli. Mol. Microbiol. 78:1577-90 |
|---|---|
| Abstract |
Survival of exposure to methylglyoxal (MG) in Gram-negative pathogens is largely dependent upon the operation of the glutathione-dependent glyoxalase system, consisting of two enzymes, GlxI (gloA) and GlxII (gloB). In addition, the activation of the KefGB potassium efflux system is maintained closed by glutathione (GSH) and is activated by S-lactoylGSH (SLG), the intermediate formed by GlxI and destroyed by GlxII. Escherichia coli mutants lacking GlxI are known to be extremely sensitive to MG. In this study we demonstrate that a ΔgloB mutant is as tolerant of MG as the parent, despite having the same degree of inhibition of MG detoxification as a ΔgloA strain. Increased expression of GlxII from a multicopy plasmid sensitizes E. coli to MG. Measurement of SLG pools, KefGB activity and cytoplasmic pH shows these parameters to be linked and to be very sensitive to changes in the activity of GlxI and GlxII. The SLG pool determines the activity of KefGB and the degree of acidification of the cytoplasm, which is a major determinant of the sensitivity to electrophiles. The data are discussed in terms of how cell fate is determined by the relative abundance of the enzymes and KefGB. |
| Links |
PubMed PMC3412212 Online version:10.1111/j.1365-2958.2010.07426.x |
| Keywords |
Escherichia coli/drug effects; Escherichia coli/enzymology; Escherichia coli/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Glutathione/analogs & derivatives; Glutathione/metabolism; Lactoylglutathione Lyase/genetics; Lactoylglutathione Lyase/metabolism; Microbial Viability; Potassium-Hydrogen Antiporters/genetics; Potassium-Hydrogen Antiporters/metabolism; Pyruvaldehyde/metabolism; Pyruvaldehyde/pharmacology |
| edit table |
Significance
You can help EcoliWiki by summarizing why this paper is useful
Useful Materials and Methods
You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.
Annotations
<annotationlinks/>
EcoliWiki Links
Add links to pages that link here (e.g. gene, product, method pages)
See also
References
See Help:References for how to manage references in EcoliWiki.