PMID:16928682: Difference between revisions

From EcoliWiki
Jump to navigation Jump to search
← Older edit
Roystefan (talk | contribs)
14 edits
Fill PMID: Page!
imported>Wikientrybot
change PMID template to TableEdit version
 
(2 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{RightTOC}}
{{RightTOC}}
<protect>
<!--box uid=d41d8cd98f00b204e9800998ecf8427e.171943.I52238d559f075-->
<span style = 'font-size: large'> '''Almeida, CC, Romão, CV, Lindley, PF, Teixeira, M and Saraiva, LM'''  (2006) The role of the hybrid cluster protein in oxidative stress defense.''J. Biol. Chem.'' '''281''':32445-50</span>
<!--
******************************************************************************************
*
*  ** PLEASE DON'T EDIT THIS TABLE DIRECTLY. Use the edit table link under the table. **
*
****************************************************************************************** -->
{|  id="I52238d559f075"  class=" tableEdit PMID_info_table" 


{|{{Prettytable}} align = 'center' width= '70%'
|-
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>Hybrid cluster proteins (HCP) contain two types of Fe/S clusters, namely a [4Fe-4S](2+/1+) or [2Fe-2S](2+/1+) cluster and a novel type of hybrid cluster, [4Fe-2S-2O], in the as-isolated state. Although first isolated from anaerobic sulfate-reducing bacteria, the analysis of the genomic sequences reveals that genes encoding putative hybrid cluster proteins are present in a wide range of organisms, aerobic, anaerobic, or facultative, from the Bacteria, Archaea, and Eukarya domains. Despite a detailed spectroscopic and structural characterization, the precise physiological function of these proteins remained unknown. The present work shows that the transcription of the Escherichia coli hcp gene is induced by hydrogen peroxide, and this induction is regulated by the redox-sensitive transcriptional activator, OxyR. The E. coli hcp mutant strain exhibits higher sensitivity to hydrogen peroxide, a behavior that reverts to the wild type phenotype once a plasmid carrying the hcp gene is reintroduced. Furthermore, the purified HCPs from E. coli and Desulfovibrio desulfuricans ATCC 27774 show an alternative enzymatic activity, which under physiological conditions exhibited K(m) values for hydrogen peroxide (approximately 0.3 mM) within the range of other peroxidases. Altogether, the results reveal that HCP is involved in oxidative stress protection.</protect>
!align=left  |Citation
||
'''Almeida, CC, Romão, CV, Lindley, PF, Teixeira, M and Saraiva, LM'''  (2006) The role of the hybrid cluster protein in oxidative stress defense. ''J. Biol. Chem.'' '''281''':32445-50
|-
|-
|{{TableHeadingColor}} nowrap |'''Links''' ||
!align=left  |Abstract
*  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=16928682 PubMed]
||
Hybrid cluster proteins (HCP) contain two types of Fe/S clusters, namely a [4Fe-4S](2+/1+) or [2Fe-2S](2+/1+) cluster and a novel type of hybrid cluster, [4Fe-2S-2O], in the as-isolated state. Although first isolated from anaerobic sulfate-reducing bacteria, the analysis of the genomic sequences reveals that genes encoding putative hybrid cluster proteins are present in a wide range of organisms, aerobic, anaerobic, or facultative, from the Bacteria, Archaea, and Eukarya domains. Despite a detailed spectroscopic and structural characterization, the precise physiological function of these proteins remained unknown. The present work shows that the transcription of the Escherichia coli hcp gene is induced by hydrogen peroxide, and this induction is regulated by the redox-sensitive transcriptional activator, OxyR. The E. coli hcp mutant strain exhibits higher sensitivity to hydrogen peroxide, a behavior that reverts to the wild type phenotype once a plasmid carrying the hcp gene is reintroduced. Furthermore, the purified HCPs from E. coli and Desulfovibrio desulfuricans ATCC 27774 show an alternative enzymatic activity, which under physiological conditions exhibited K(m) values for hydrogen peroxide (approximately 0.3 mM) within the range of other peroxidases. Altogether, the results reveal that HCP is involved in oxidative stress protection.
|-
!align=left  |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=16928682 PubMed]
Online version:[http://dx.doi.org/10.1074/jbc.M605888200 10.1074/jbc.M605888200]
Online version:[http://dx.doi.org/10.1074/jbc.M605888200 10.1074/jbc.M605888200]
|-
!align=left  |Keywords
||
Desulfovibrio desulfuricans; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Gene Deletion; Genes, Bacterial; Genetic Complementation Test; Hydrogen Peroxide/pharmacology; Iron-Sulfur Proteins/chemistry; Iron-Sulfur Proteins/genetics; Iron-Sulfur Proteins/metabolism; Models, Chemical; Oxidants/pharmacology; Oxidation-Reduction; Oxidative Stress; Plasmids; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Regulon/genetics; Trans-Activators/genetics; Trans-Activators/metabolism; Transcription, Genetic
|- class="tableEdit_footer"
|<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.171943.I52238d559f075&page=171943&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> ||
|}
|}
</protect>
<!--box uid=d41d8cd98f00b204e9800998ecf8427e.171943.I52238d559f075-->
==Significance {{HelpIcon|Help:Literature}} ==
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}
{{LitSignificance}}
Line 19: Line 38:


==Annotations {{HelpIcon|Help:Literature}}==
==Annotations {{HelpIcon|Help:Literature}}==
<protect><!--box uid=63ce1649aab8b3180235b0af7618f667.171943.T4bdf5add76e2d-->
<protect><annotationlinks/></protect>
<!--
******************************************************************************************
*
*  ** PLEASE DON'T EDIT THIS TABLE DIRECTLY.  Use the edit table link under the table. **
*
****************************************************************************************** -->
{|  id="T4bdf5add76e2d"  class=" tableEdit GO_table_reference" 
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
 
|- class="tableEdit_footer"
|<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.171943.T4bdf5add76e2d&page=171943&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table]</span> || || || || || || || ||
|}
<!--box uid=63ce1649aab8b3180235b0af7618f667.171943.T4bdf5add76e2d--></protect>


==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
==EcoliWiki Links {{HelpIcon|Help:Literature}} ==

Latest revision as of 04:30, 15 September 2013

Citation

Almeida, CC, Romão, CV, Lindley, PF, Teixeira, M and Saraiva, LM (2006) The role of the hybrid cluster protein in oxidative stress defense. J. Biol. Chem. 281:32445-50

Abstract

Hybrid cluster proteins (HCP) contain two types of Fe/S clusters, namely a [4Fe-4S](2+/1+) or [2Fe-2S](2+/1+) cluster and a novel type of hybrid cluster, [4Fe-2S-2O], in the as-isolated state. Although first isolated from anaerobic sulfate-reducing bacteria, the analysis of the genomic sequences reveals that genes encoding putative hybrid cluster proteins are present in a wide range of organisms, aerobic, anaerobic, or facultative, from the Bacteria, Archaea, and Eukarya domains. Despite a detailed spectroscopic and structural characterization, the precise physiological function of these proteins remained unknown. The present work shows that the transcription of the Escherichia coli hcp gene is induced by hydrogen peroxide, and this induction is regulated by the redox-sensitive transcriptional activator, OxyR. The E. coli hcp mutant strain exhibits higher sensitivity to hydrogen peroxide, a behavior that reverts to the wild type phenotype once a plasmid carrying the hcp gene is reintroduced. Furthermore, the purified HCPs from E. coli and Desulfovibrio desulfuricans ATCC 27774 show an alternative enzymatic activity, which under physiological conditions exhibited K(m) values for hydrogen peroxide (approximately 0.3 mM) within the range of other peroxidases. Altogether, the results reveal that HCP is involved in oxidative stress protection.

Links

PubMed Online version:10.1074/jbc.M605888200

Keywords

Desulfovibrio desulfuricans; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Gene Deletion; Genes, Bacterial; Genetic Complementation Test; Hydrogen Peroxide/pharmacology; Iron-Sulfur Proteins/chemistry; Iron-Sulfur Proteins/genetics; Iron-Sulfur Proteins/metabolism; Models, Chemical; Oxidants/pharmacology; Oxidation-Reduction; Oxidative Stress; Plasmids; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Regulon/genetics; Trans-Activators/genetics; Trans-Activators/metabolism; Transcription, Genetic

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.

Retrieved from "https://ecoliwiki.org/colipedia/index.php?title=PMID:16928682&oldid=1461759"