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Peptidyl transferase activity in wheat germ ribosomes. Effect of some antibiotics
Biochimica Et Biophysica Acta
|March 2, 1977
Abstract:
The formation of N-acetyl-leucyl-puromycin in a "fragment reaction" catalyzed by 80 S ribosomes from wheat germ was characterized. The reaction product was identified by high-voltage electrophoresis. The fragment reaction is inhibited by sparsomycin, blasticidin S, gougerotin and to a lesser degree by amicetin and tetracycline. Formation of an acLeu-pentanucleotide-ribosomes complex was strongly stimulated by sparsomycin.
Insights
Wheat germ ribosomes catalyze N-acetyl-leucyl-puromycin formation. Antibiotics like sparsomycin inhibit this fragment reaction, while sparsomycin also stimulates a key complex formation.
Area of Science:
- Molecular Biology
- Biochemistry
- Ribosome Function
Background:
- Ribosomes are essential cellular machinery responsible for protein synthesis.
- Understanding ribosome-catalyzed reactions, like fragment reactions, is crucial for deciphering translation mechanisms.
Purpose of the Study:
- To characterize the formation of N-acetyl-leucyl-puromycin via a fragment reaction.
- To investigate the effects of specific antibiotics on this ribosome-catalyzed process.
Main Methods:
- Utilized 80 S ribosomes isolated from wheat germ.
- Employed high-voltage electrophoresis for reaction product identification.
- Assessed the inhibitory effects of various antibiotics on the fragment reaction.
Main Results:
- Successfully characterized the formation of N-acetyl-leucyl-puromycin.
- Identified sparsomycin, blasticidin S, and gougerotin as potent inhibitors.
- Observed that amicetin and tetracycline showed lesser inhibitory effects.
- Found strong stimulation of an acLeu-pentanucleotide-ribosomes complex by sparsomycin.
Conclusions:
- The fragment reaction catalyzed by wheat germ 80 S ribosomes is sensitive to specific antibiotics.
- Sparomycin exhibits a dual role, inhibiting the reaction while stimulating complex formation, suggesting intricate regulatory mechanisms.