ArticleThe Journal of biological chemistry2009
Regulation by glutathionylation of isocitrate lyase from Chlamydomonas reinhardtii.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 41 citations in OpenAlex.
- Chloroplasts lacking class I glutaredoxins are functional but show a delayed recovery of protein cysteinyl redox state after oxidative challenge.Redox biology · 2024Article
- Chlamydomonas as a model for reactive oxygen species signaling and thiol redox regulation in the green lineage.Plant physiology · 2021Review
- Function and Regulation of Chloroplast Peroxiredoxin IIE.Antioxidants (Basel, Switzerland) · 2021Article
- Strategies to Study Dark Growth Deficient or Slower Mutants in Chlamydomonas reinhardtii.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Structural and Biochemical Insights into the Reactivity of Thioredoxin h1 fromAntioxidants (Basel, Switzerland) · 2019Article
- Role of Glyoxylate Shunt in Oxidative Stress Response.The Journal of biological chemistry · 2016Article
- Biochemical Validation of the Glyoxylate Cycle in the Cyanobacterium Chlorogloeopsis fritschii Strain PCC 9212.The Journal of biological chemistry · 2015Article
- Insight into protein S-nitrosylation in Chlamydomonas reinhardtii.Antioxidants & redox signaling · 2014Article
- S-glutathionylation of ion channels: insights into the regulation of channel functions, thiol modification crosstalk, and mechanosensing.Antioxidants & redox signaling · 2014Review
- Redox regulation of the Calvin-Benson cycle: something old, something new.Frontiers in plant science · 2013Review
- The Synechocystis PCC6803 MerA-like enzyme operates in the reduction of both mercury and uranium under the control of the glutaredoxin 1 enzyme.Journal of bacteriology · 2013Article
- Glutathionylation in the photosynthetic model organism Chlamydomonas reinhardtii: a proteomic survey.Molecular & cellular proteomics : MCP · 2012Article
- Protein S-glutathionylation in malaria parasites.Antioxidants & redox signaling · 2011Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Post-translational modification of protein cysteine residues is emerging as an important regulatory and signaling mechanism. We have identified numerous putative targets of redox regulation in the unicellular green alga Chlamydomonas reinhardtii. One enzyme, isocitrate lyase (ICL), was identified both as a putative thioredoxin target and as an S-thiolated protein in vivo. ICL is a key enzyme of the glyoxylate cycle that allows growth on acetate as a sole source of carbon. The aim of the present study was to clarify the molecular mechanism of the redox regulation of Chlamydomonas ICL using a combination of biochemical and biophysical methods. The results clearly show that purified C. reinhardtii ICL can be inactivated by glutathionylation and reactivated by glutaredoxin, whereas thioredoxin does not appear to regulate ICL activity, and no inter- or intramolecular disulfide bond could be formed under any of the conditions tested. Glutathionylation of the protein was investigated by mass spectrometry analysis, Western blotting, and site-directed mutagenesis. The enzyme was found to be protected from irreversible oxidative inactivation by glutathionylation of its catalytic Cys(178), whereas a second residue, Cys(247), becomes artifactually glutathionylated after prolonged incubation with GSSG. The possible functional significance of this post-translational modification of ICL in Chlamydomonas and other organisms is discussed.
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