Work

Control of eIF-2 phosphatase activity in rabbit reticulocyte lysate.

Year: 1979

Type: article

Abstract: A sensitive assay requiring picomole amounts of [32P]eIF-2 to measure eIF-2 phosphatase activity has been developed. Dephosphorylation of [32P]eIF-2 alpha (38,000-dalton subunit) is extremely rapid (t 1/2 = 20 sec) and occurs at the same rate in both hemin-supplemented and hemin-depleted lysates. In contrast, [32P]eIF-2 beta phosphate is stable under all conditions studied. At concentrations required to produce a transient inhibition of protein synthesis, GDP prevents dephosphorylation of half of the phosphate introduced on eIF-2 alpha by the hemin-controlled repressor. Equimolar GTP is without effect. The concept that the energy charge of the guanylate pool may regulate accessibility of a phosphorylated site on eIF-2 alpha to its phosphatase and the implication of this to the mechanism of hemin-regulated translational control are discussed.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.76.3.1094

Authors: B Safer, R Jagus

Institutions: National Institutes of Health, National Heart, Lung, and Blood Institute

Language: English

Topic: RNA and protein synthesis mechanisms

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

OpenAlex ID: W2034510876

FWCI: 5.151

Cites: 29

Cited by: 55

Related to: 10