A functional interaction between methionyl-transfer RNA hydrolase and a transfer RNA binding factor |
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Authors: | J.M. Cimadevilla J. Morrisey B. Hardesty |
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Affiliation: | Clayton Foundation Biochemical Institute and Department of Chemistry The University of Texas Austin, Texas 78712, U.S.A. |
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Abstract: | Met-tRNAf bound at low Mg ion concentrations to rabbit reticulocyte 40 S ribosomal subunits in the presence of ApUpG and a eukaryotic tRNA binding factor serves readily as a substrate for a Met-tRNA hydrolase from rabbit reticulocytes. This hydrolysis occurs rapidly at 0 °C, appears to be specific for Met-tRNAf, and is not inhibited by 60 S ribosomal subunits. These reactions may be responsible for the accumulation of deacylated tRNAfMet observed in ribosomes isolated from sodium fluoride-treated cells. |
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