Stress-Induced Protein S-Glutathionylation in Arabidopsis
نویسندگان
چکیده
منابع مشابه
Stress-induced protein S-glutathionylation in Arabidopsis.
S-Glutathionylation (thiolation) is a ubiquitous redox-sensitive and reversible modification of protein cysteinyl residues that can directly regulate their activity. While well established in animals, little is known about the formation and function of these mixed disulfides in plants. After labeling the intracellular glutathione pool with [35S]cysteine, suspension cultures of Arabidopsis (Arab...
متن کاملStress-Induced Protein S-Glutathionylation and S-Trypanothionylation in African Trypanosomes—A Quantitative Redox Proteome and Thiol Analysis
AIMS Trypanosomatids have a unique trypanothione-based thiol redox metabolism. The parasite-specific dithiol is synthesized from glutathione and spermidine, with glutathionylspermidine as intermediate catalyzed by trypanothione synthetase. In this study, we address the oxidative stress response of African trypanosomes with special focus on putative protein S-thiolation. RESULTS Challenging bl...
متن کاملNitrosative stress-induced s-glutathionylation of protein disulfide isomerase leads to activation of the unfolded protein response.
The rapid proliferation of cancer cells mandates a high protein turnover. The endoplasmic reticulum (ER) is intimately involved in protein processing. An accumulation of unfolded or misfolded proteins in the ER leads to a cascade of transcriptional and translational events collectively called the unfolded protein response (UPR). Protein disulfide isomerase (PDI) is one of the most abundant ER p...
متن کاملSignalling by NO-induced protein S-nitrosylation and S-glutathionylation: convergences and divergences.
The role of nitric oxide in several signalling routes has been clearly established. In recent years increasing attention has been paid to its ability to produce covalent protein post-translational modifications in conjunction with other reactive oxygen and nitrogen species. Among these, the modification of cysteine residues has been shown to be of particular importance due to the functional rel...
متن کاملPrediction of S-Glutathionylation Sites Based on Protein Sequences
S-glutathionylation, the reversible formation of mixed disulfides between glutathione(GSH) and cysteine residues in proteins, is a specific form of post-translational modification that plays important roles in various biological processes, including signal transduction, redox homeostasis, and metabolism inside cells. Experimentally identifying S-glutathionylation sites is labor-intensive and ti...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Plant Physiology
سال: 2005
ISSN: 1532-2548,0032-0889
DOI: 10.1104/pp.104.058917