PMID: 7030409Aug 1, 1981Paper

The regulation of eIF-2 function protein synthesis initiation

Biochimie
B Safer, R Jagus

Abstract

The regulation of eIF-2 activity during protein synthesis initiation has been postulated to involve phosphorylation/dephosphorylation mechanisms and/or the participation of ancillary protein factors. Both mechanisms would affect directly the binding of initiator methionyl-tRNAi by eIF-2. Recent data concerning the phosphorylation state of eIF-2 in hemin-deficient lysates and other covalent modifications which alter the efficiency of eIF-2 utilization, however, suggest that modulation of eIF-2 activity is more complex, and involves alteration of its catalytic recycling.

References

Mar 1, 1979·Proceedings of the National Academy of Sciences of the United States of America·B Safer, R Jagus
May 1, 1979·Proceedings of the National Academy of Sciences of the United States of America·C de Haro, S Ochoa
Oct 1, 1979·Proceedings of the National Academy of Sciences of the United States of America·A DasN K Gupta
Sep 21, 1978·Biochimica Et Biophysica Acta·Y Kaziro
Sep 20, 1976·Biochimica Et Biophysica Acta·G M Walton, G N Gill
Jan 1, 1981·Progress in Nucleic Acid Research and Molecular Biology·R JagusB Safer
Jan 1, 1981·Proceedings of the National Academy of Sciences of the United States of America·J SiekierkaS Ochoa
Oct 30, 1981·Biochemical and Biophysical Research Communications·T H Jones, M Gupta
May 28, 1980·Molecular and Cellular Biochemistry·M Gross

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