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Plant and Cell Physiology, 1986, Vol. 27, No. 1 177-182
© 1986

Short Communication

Protein Synthesis Linked to Respiration and Phosphorylation in Intact Euglena Mitochondria

Evelyne Delorme1, Benito Gomez-Silva2, Arthur I. Stern3 and Jerome A. Schiff

Institute for Photobiology, Brandeis University Waltham, MA 02254, U.S.A.

Highly purified condensed mitochondria obtained from bleached mutant. W10BSmL of Euglena gracilis Klebs var bacillaris Cori incorporate [35S]methionine into protein when fortified with malate, ADP, Mg2+, phosphate and a sucrose osmoticum. Twenty to twenty-five polypeptide bands were found to be labeled in organello when the labeled protein was subjected to sodium dodecylsulfate polyacrylamide gel electrophoresis. Methionine incorporation, but not respiration or oxidative phosphorylation, was blocked by chloramphenicol and other 70S ribosomal translation inhibitors but cycloheximide and ribonuclease were without effect. Inhibitors of electron transport and uncouplers of oxidative phosphorylation were excellent inhibitors of protein synthesis. Thus, these mitochondrial preparations carry out protein synthesis in organello that is linked to respiration and oxidative phosphorylation.

1Present address: VA Hospital Outpatient Clinic, 17 Court St., Boston, MA 02115, U.S.A.

2Present address: Laboratories de Microbiologia e Inmunologia, Universidad Catolica de Chile, Casilla 114-D, Santiago, Chile.

3Present address: Botany Department, University of Massachusetts, Amherst, MA 01003, U.S.A.

(Received June 17, 1985; Accepted October 28, 1985)
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