English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

A mechanism based on reversible phosphorylation of the  α -subunit of eukaryotic initiation factor 2 (eIF2 α ) has been confirmed as an important regulatory pathway for the inhibition of protein synthesis in mammalian and yeast cells, while plants constitute the significant exception. We studied the induction of  Ta eIF2 α  phosphorylation in germinated wheat ( Triticum aestivum ) embryos subjected to different adverse conditions. Data confirmed that formation of  Ta eIF2( α P) was not a general response, as no phosphorylation was observed under salt, oxidative, or heat stress. Nevertheless, treatment by salicylic acid, UV-light, cold shock and histidinol did induce phosphorylation of  Ta eIF2 α  of wheat as has been established previously for  At eIF2 α  in Arabidopsis ( Arabidopsis thaliana ). The influence of  Ta eIF2 α  phosphorylation on translation of reporter mRNA with different 5′-untranslated regions (5′UTRs) was studied in wheat germ cell-free system (WG-CFS), in which  Ta eIF2 α  was first phosphorylated either by heterologous recombinant human protein kinase,  Hs PKR (activated by double-stranded (ds)RNA), or by endogenous protein kinase  Ta GCN2 (activated by histidinol). Pretreatment of WG-CFS with  Hs PKR in the presence of dsRNA or with histidinol resulted in intense phosphorylation of  Ta eIF2 α ; however, the translation levels of all tested mRNAs decreased by only 10–15% and remained relatively high. In addition, factor  Oc eIF2 from rabbit ( Oryctolagus cuniculus ) bound GDP much more strongly than the homologous factor  Ta eIF2 from wheat germ. Furthermore, factor  Oc eIF2B was able to stimulate guanine nucleotide exchange (GDP→GTP) on  Oc eIF2 but had no effect on a similar exchange on  Ta eIF2. These results suggest that the mechanism of stress response  via  eIF2 α  phosphorylation is not identical in all eukaryotes, and further research is required to find and study in detail new plant-specific mechanisms that may inhibit overall protein synthesis in plants under stress.

Evidence That Phosphorylation of the α-Subunit of eIF2 Does Not Essentially Inhibit mRNA Translation in Wheat Germ Cell-Free System