Partial reaction of peptide initiation inhibited by phosphorylation of either initiation factor eIF-2 or 40S ribosomal proteins.
- 1 April 1977
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 74 (4) , 1445-1449
- https://doi.org/10.1073/pnas.74.4.1445
Abstract
Preparations of the hemin-controlled repressor (HCR) from rabbit reticulocytes contain cyclic AMP-independent protein kinase activity for the smallest subunit of the peptide initiation factor eIF-2 and for proteins of reticulocyte 40S ribosomal subunits. Binding of the ternary complex formed between Met-tRNAf, GTP and eIF-2 to 40S ribosomal subunits is inhibited by phosphorylation of either the ribosomal subunits or eIF-2. The protein kinase activity responsible for phosphorylation of eIF-2 was separated from the activity for phosphorylation of 40S ribosomal subunits and shown to independently block the same partial reaction of peptide initiation. Different enzymes are apparently involved, each capable of regulating peptide initiation at the same step but by a different mechanism.This publication has 31 references indexed in Scilit:
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