Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2007-2-12
pubmed:abstractText
Glutaredoxins (Grxs) are small ubiquitous glutathione-disulfide oxidoreductase that reduce disulfide bonds of target proteins and maintain the redox homoeostasis of cells. Disruption of ssr2061 reduced the viability of cells indicated Grx2061 has a protective role against oxidative stress in Synechocystis sp. PCC 6803. To understand the function of Grx2061 in cyanobacteria and its difference from plant, Grx targets were retained specifically on an affinity media coupled with a mutated monocysteinic Grx and identified by mass spectra. Among 42 identified targets, 26 of them are novel ones compared with those known in higher plants. These proteins are supposed to be involved in 12 cellular processes including oxidative stress response, Calvin cycle, protein synthesis, and etc. Biochemical tests highlighted four of them which showed a Grx-dependent activation of peroxiredoxin and deactivation of catalase. Oxidized Grx2061 could keep redox equilibrium with another probable Grx and be reduced by thioredoxin reductase, indicating that Grx2061 can accept electrons from either glutathione or thioredoxin reductase. Our studies suggest Grx2061 in cyanobacteria plays an important role in redox network and its targets are as extensive as that in other organisms.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
458
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
220-8
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Identification of novel targets of cyanobacterial glutaredoxin.
pubmed:affiliation
Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't