PMID: 3756169Oct 16, 1986Paper

Reduced turnover of the elongation factor EF-1 X ribosome complex after treatment with the protein synthesis inhibitor II from barley seeds

Biochimica Et Biophysica Acta
L NilssonO Nygård

Abstract

The effect of the protein synthesis inhibitor II from barley seeds (Hordeum sp.) on protein synthesis was studied in rabbit reticulocyte lysates. Inhibitor treatment of the lysates resulted in a rapid decrease in amino acid incorporation and an accumulation of heavy polysomes, indicating an effect of the inhibitor on polypeptide chain elongation. The protein synthesis inhibition was due to a catalytic inactivation of the large ribosomal subunit with no effect on the small subparticle. The inhibitor-treated ribosomes were fully active in participating in the EF-1-dependent binding of [14C]phenylalanyl-tRNA to poly(U)-programmed ribosomes in the presence of GTP and the binding of radioactively labelled EF-2 in the presence of GuoPP[CH2]P. Furthermore, the ribosomes were still able to catalyse peptide-bond formation. However, the EF-1- and ribosome-dependent hydrolysis of GTP was reduced by more than 40% in the presence of inhibitor-treated ribosomes, while the EF-2- and ribosome-dependent GTPase remained unaffected. This suggests that the active domains involved in the two different GTPases are non-identical. Treatment of reticulocyte lysates with the barley inhibitor resulted in a marked shift of the steady-state distribution of...Continue Reading

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Citations

Nov 18, 2005·Die Naturwissenschaften·Pier Luigi LuisiPasquale Stano
Jul 1, 1990·APMIS : Acta Pathologica, Microbiologica, Et Immunologica Scandinavica·M G BattelliF Stirpe
May 5, 2001·Annual Review of Plant Physiology and Plant Molecular Biology·Kirsten Nielsen, Rebecca S Boston
Nov 10, 2011·Toxins·Assaf Shapira, Itai Benhar
Jan 1, 1990·Progress in Growth Factor Research·D A Lappi, A Baird
Jul 1, 1992·Experimental Cell Research·M G BattelliF Stirpe

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