N-Formylmethionyl-tRNAf of Wheat Chloroplasts. Its Synthesis by a Wheat Transformylase

Jonathan P. Leis, Elizabeth B. Keller*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

18 Scopus citations

Abstract

In a study of the role of methionine in protein chain initiation in wheat, a transformylase was isolated and partially purified from commercial wheat germ and from wheat leaves grown under sterile conditions. This enzyme catalyzed the formylation of a methionyl-tRNAf which was present in the wheat leaf chloroplasts. The enzyme used N10-formyltetrahydrofolate as formyl donor and required 5 mM Mg2+ and 20 mM K+ ions for maximum activity. The molecular weight of the transformylase was estimated at 45,000 by gel filtration on Sephadex G-150. The enzyme was present in isolated chloroplasts at a higher specific activity than in the remainder of the leaf extract. This transformylase and the methionyl-tRNAf are components of a protein chain initiating system in wheat chloroplasts similar in many ways to the system in Escherichia coli.

Original languageEnglish (US)
Pages (from-to)889-894
Number of pages6
JournalBiochemistry
Volume10
Issue number5
DOIs
StatePublished - Mar 1 1971

ASJC Scopus subject areas

  • Biochemistry

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