Glutathione. V. The effects of the thiol-oxidizing agent diamide on initiation and translation in rabbit reticulocytes

Tova Zehavi-Willner, Edward M. Kosower, Tim Hunt, Nechama S. Kosower

Research output: Contribution to journalArticlepeer-review

Abstract

1. 1. Addition of the thiol-oxidizing agent, diamide ((CH3)2NCON=NCON(CH3)2), to rabbit reticulocytes, which are actively synthesizing protein, halts instantaneously the incorporation of labeled amino acid into soluble protein along with the oxidation of glutathione (GSH) to the disulfide (GSSG). 2. 2. Both translation and initiation are affected. 3. 3. Processes involved in translation (and release) recover after a short lag, following regeneration of 40-60 % of the original GSH. 4. 4. Initiation is more sensitive than translation to treatment with diamide, recovers after regeneration of 70-80 % of the original GSH, but after long periods of zero GSH, only incompletely. 5. 5. The rapidity of the response of the protein synthesizing system to diamide treatment suggests that thiol groups are intimately and directly linked to various stages in protein synthesis. 6. 6. The remarkable reversibility observed in protein synthesis after diamide treatment offers a new probe into the details of the complex process.

Original languageEnglish
Pages (from-to)245-251
Number of pages7
JournalBBA Section Nucleic Acids And Protein Synthesis
Volume228
Issue number1
DOIs
StatePublished - 1 Jan 1971
Externally publishedYes

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