PMID: 7032598Dec 28, 1981Paper

Purification and properties of fMet-tRNAf deacylase from Escherichia coli

Biochimica Et Biophysica Acta
K IgarashiS Hirose

Abstract

A formylmethionyl-tRNAf deacylase has been purified about 330-fold from a crude initiation factor preparation (1 M NH4Cl ribosomal wash) from Escherichia coli Q13. The enzyme was nearly homogeneous and had an apparent molecular weight of 24 000. Rat liver methionyl-tRNAf and E. coli methionyl-tRNAm were not hydrolyzed significantly by the enzyme under standard conditions. Q beta RNA- and AUG(A)n-directed polypeptide synthesis was inhibited by the enzyme. The inhibition was at the level of initiation of polypeptide synthesis. The enzymatic activity was inhibited by various factors necessary for polypeptide synthesis. The activity was inhibited more by NH4Cl and spermidine than by Mg2+, GTP and ATP. The complex of formylmethionyl-tRNAf, initiation factor 2 and GTP was resistant to enzymatic hydrolysis, and the resistance was enhanced by the addition of AUG and ribosomes to the above reaction mixture.

References

Mar 11, 1975·Biochemistry·K E Smith, E C Henshaw
Jan 15, 1973·European Journal of Biochemistry·R BenneH O Voorma
Oct 2, 1974·European Journal of Biochemistry·K IgarashiS Hirose
Mar 15, 1974·Journal of Molecular Biology·J M CimadevillaB Hardesty
Mar 19, 1970·Biochimica Et Biophysica Acta·H Kössel
Oct 15, 1970·Biochimica Et Biophysica Acta·J R MenningerW S Stirewalt
Sep 1, 1972·Archives of Biochemistry and Biophysics·J Morrisey, B Hardesty
Mar 28, 1980·Biochemical and Biophysical Research Communications·K IgarashiS Hirose
Apr 14, 1956·Nature·A GIERER, G SCHRAMM
Mar 15, 1961·Proceedings of the National Academy of Sciences of the United States of America·T LOEB, N D ZINDER

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