NDLI: Regulation of protein synthesis in rabbit reticulocyte lysates by the heme-regulated protein kinase: Inhibition of interaction of $Met-tRNA_{f}^{Met}$ binding factor with another initiation factor in formation of $Met-tRNA_{f}^{Met}·40S$ ribosomal subunit complexes

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Human mitochondrial DNA: analysis of 7S DNA from the origin of replication.

Regulation of protein synthesis in rabbit reticulocyte lysates by the heme-regulated protein kinase: Inhibition of interaction of $Met-tRNA_{f}^{Met}$ binding factor with another initiation factor in formation of $Met-tRNA_{f}^{Met}·40S$ ribosomal subunit complexes

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Repair of depurinated DNA in vitro by enzymes purified from human lymphoblasts.

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Regulation of protein synthesis in rabbit reticulocyte lysates by the heme-regulated protein kinase: Inhibition of interaction of $Met-tRNA_{f}^{Met}$ binding factor with another initiation factor in formation of $Met-tRNA_{f}^{Met}·40S$ ribosomal subunit complexes

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Das, A. Dasgupta, A. London, I. M. Ralston, R. Ranu, R. S. Roy, R. Majumdar, A. Gupta, N. K.
Abstract	Protein synthesis in reticulocytes and their lysates is regulated by heme. In heme deficiency a heme-regulated translational inhibitor (HRI) that blocks initiation of polypeptide chains is activated. HRI is a protein kinase (ATP: protein phosphotransferase, EC 2.7.1.37) that specifically phosphorylates the 38,000-dalton subunit of the Met-tRNA(f) (Met) binding factor (IF), which forms a ternary complex with Met-tRNA(f) (Met) and GTP, a finding that suggests that the inhibition by HRI involves the phosphorylation of IF. We have investigated the effect of HRI in the partial reactions of protein chain initiation in which the IF-promoted binding of Met-tRNA(f) (Met) to 40S ribosomal subunits is enhanced by another initiation factor [ternary complex dissociation factor (TDF)] and AUG. The results show that HRI at very low concentrations markedly inhibits the binding of Met-tRNA(f) (Met) to 40S subunits. The inhibitory effect of HRI requires ATP. Under these conditions HRI phosphorylates only the 38,000-dalton subunit of IF. The TDF preparations not only promote the binding of the ternary complex to 40S subunits but also promote the dissociation of the ternary complex in the presence of 5 mM Mg(2+) at 0 degrees . The preincubation of purified IF alone with low concentrations of HRI and ATP does not significantly affect its capacity to form the ternary complex; however, the TDF-promoted dissociation of the ternary complex is inhibited. The nonhydrolyzable analog adenosine 5'-[beta,gamma-imido]triphosphate does not substitute for ATP. These findings suggest that phosphorylation causes a conformational modification in IF, which results in inhibition of the interaction between the ternary complex and TDF that is required for the binding of the ternary complex to 40S subunits.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	2
Volume Number	75
Language	English
Publisher	National Academy of Sciences
Publisher Date	1978-05-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Heme Metabolism Methionine Peptide Initiation Factors Protein Kinases RNA, Transfer Ribosomes Adenosine Triphosphate Animals Magnesium Peptide Chain Initiation, Translational Phosphates Protein Biosynthesis Rabbits Reticulocytes Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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