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Nucleic Acids Research, 1975, Vol. 2, No. 11 2119-2130
© 1975

Articles

Specific hydrolysis of methionyl-tRNAfMet catalyzed by a purified peptide initiation factor from rat liver

Jan Hradec

Department of Biochemistry, Oncological Institute 180 00 Prague 8, Czechoslovakia

Received October 6, 1975. A peptide initiation factor purified from rat liver and promoting the binding of initiator tRNA and model initiators to 40S and 80S ribosomes at an acid pH liberates methionine and N-acetylmethionine from tRNAfMet at neutral reaction. Phenylalanyl-tRNA, N-acetylphenylalanyl-tRNA and methionyl-tRNAfMet are not hydrolyzed under the same conditions. Hydrolysis of methionyl-tRNAfMet is stimulated by the presence of the 40S ribosomal subunit and proceeds at 37°C until all the substrate has been split No hydrolysis of initiator tRNA or N-acetylmethionyl-tRNAfMet, occurrs at 0°C. Hydrolysis is slightly stimulated by GTP and Mg2+ but not by KCl. The binding and hydrolyzing activity associated with a single protein factor may have an important function in regulating the rate of peptide initiation.


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