Studies on the ability of norleucine to replace methionine in the initiation of protein synthesis in E. coli

It has been previously shown that norleucine can acylate both tRNA F Met and tRNA F Met and be converted to fNorleu-tRNA F Met. The present studies have compared the reactivity of fNorleu-tRNA F Met with fMet-tRNA F Met in various reactions associated with protein synthesis. No significant differenc...

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Veröffentlicht in:Archives of biochemistry and biophysics 1970-12, Vol.141 (2), p.525-532
Hauptverfasser: Kerwar, S.S., Weissbach, Herbert
Format: Artikel
Sprache:eng
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Zusammenfassung:It has been previously shown that norleucine can acylate both tRNA F Met and tRNA F Met and be converted to fNorleu-tRNA F Met. The present studies have compared the reactivity of fNorleu-tRNA F Met with fMet-tRNA F Met in various reactions associated with protein synthesis. No significant differences were observed in the binding to ribosomes, reaction with puromycin, and deformylation reaction. However, unlike methionine, norleucine was not able to repress any of the enzymes involved in methionine synthesis.
ISSN:0003-9861
1096-0384
DOI:10.1016/0003-9861(70)90170-0