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J. Biochem, 1977, Vol. 81, No. 5 1347-1355
© 1977 Japanese Biochemical Society

research-article

Studies on Rat Liver Catalase

IX. Role of Methionine in Polypeptide Chain Initiation1

Terufumi SAKAMOTO and Tokuhiko HIGASHI

Department of Biochemistry, School of Pharmaceutical Sciences Showa University, Shinagawa-ku, Tokyo 142

Initiation with methionine of the synthesis of rat liver catalase [EC 1.11.1.6 [EC] ] has been investigated. Analysis of the N-terminal residue of nascent catalase peptides labeled in vivo with injected radioactive amino acids, including [3H]methionine, indicated a remarkably high content of methionine. By fractionating [3H]methionine-labeled nascent catalase according to chain length, it was found that peptides of shorter chain length contained more N-terminal methionine relative to total methionine incorporated. In addition, only a small amount of [3H]methionine was detected as the N-terminal amino acid when newly completed catalase was examined by Edman degradation. These results indicate that the synthesis of liver catalase is initiated with methionine, and suggest the presence of a mechanism for its subsequent removal from the N-terminal position.

Catalase was also synthesized in a cell-free system directed by the catalase mRNA, using [3H]Met-tRNAf or [3H]Met-tRNAm. The results obtained in such in vitro experiments were in good agreement with those from in vivo studies, and further showed that the N-terminal methionine was provided by a specific initiator tRNA, i.e. tRNAfMet.

1 This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan, for which the authors are greatly indebted.


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