Allosteric regulation of eukaryotic initiation factor eIF-2B by adenine nucleotides

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Previous studies have shown that eIF-2B purified from rabbit reticulocytes binds ATP and that the binding is prevented by NADP+. Because NADP+ inhibits the activity of eIF-2B in and vitro reactions we have examined whether or not the activity of eIF-2B is modulated by ATP. In these studies, eIF-2B, purified from rat liver, was incubated with ATP prior to assay. We found that the activity of eIF-2B was inhibited with an IC50 of approximately 0.8 mM. The inhibition was not due to phosphorylation of the factor. However, the inhibition of eIF-2B activity caused by ATP could be prevented by coincubation with either NADPH or fructose-1,6-bisphosphate. The activity of eIF-2B was also inhibited following addition of either ATP or AMPPNP to a post-mitochondrial supernatant prepared from rat liver. Therefore, it is possible that the activity of eIF-2B might be allosterically regulated in vivo not only by changes in the redox slate of pyridine dinucleotides but also by changes in the relative amounts of NADPH and ATP.

Original languageEnglish (US)
Pages (from-to)1074-1081
Number of pages8
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - 1995

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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