Synthesis of actin-like protein in rat liver mitochondria.
Isolated rat liver mitochondria failed to exhibit in vitro incorporation of [14C]-amino acids into actin-like protein. The use of a pulse-labelling technique demonstrated the appearance of [14C]-actin-like protein in the mitochondria of control, cycloheximide-free rats. The actin-like protein was identified by the method of affinity binding on DNAse1-sepharose and by electrophoresis on polyacrylamide gel with sodium dodecyl sulphate. It was shown that mitochondrial actin-like protein is not included among the nine polypeptides synthesized in mitochondria during cycloheximide-induced blockade of cytoplasmic protein synthesis. It was shown that actin-like protein was not desorbed from mitochondria by repeated washing with isotonic sucrose-mannitol medium. The results obtained indicate that the actin-like protein is biosynthesised in the cytoplasmic compartment.
D000199:Actins / Q000096:biosynthesis* / Q000302:isolation & purification; D000818:Animals; D002846:Chromatography, Affinity; D003513:Cycloheximide / Q000494:pharmacology; D003593:Cytoplasm / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D066298:In Vitro Techniques; D008297:Male; D008930:Mitochondria, Liver / Q000378:metabolism*; D014176:Protein Biosynthesis; D051381:Rats
D000199:Actins; D003513:Cycloheximide