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PMID: 193100 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Partial reaction of peptide initiation inhibited by phosphorylation of either initiation factor eIF-2 or 40S ribosomal proteins.

Kramer G, Henderson AB, Pinphanichakarn P, Wallis MH, Hardesty B

Abstract

Preparations of the hemin-controlled repressor (HCR) from rabbit reticulocytes contain 3':5'-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 shown to be inhibited by phosphorylation of either the ribosomal subunits or eIF-2. The protein kinase activity responsible for phosphorylation of eIF-2 has been separated from the activity for phosphorylation of 40S ribosomal subunits and shown to independently block the same partial reaction of peptide initiation. It appears that different enzymes are involved, each capable of regulating peptide initiation at the same step but by a different mechanism.

MeSH Terms
Animals Cyclic AMP/pharmacology Enzyme Activation Hemin/physiology Kinetics Methionine Peptide Chain Initiation, Translational Peptide Initiation Factors/isolation & purification Protein Kinases/metabolism RNA, Transfer/metabolism Rabbits Reticulocytes/enzymology Ribosomal Proteins/isolation & purification,metabolism
Chemicals
Peptide Initiation Factors Ribosomal Proteins Hemin RNA, Transfer Methionine Cyclic AMP Protein Kinases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Kramer G
Henderson A B
Pinphanichakarn P
Wallis M H
Hardesty B
References (31)
31 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1977-04-00
Pages
1445-9
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC430792
Subset
IM
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