Acetylation of Reticulocyte Ribosomal Proteins at Time of Protein Biosynthesis
AUTOR(ES)
Liew, C. C.
RESUMO
When rabbit reticulocytes were incubated in vitro with [3H]acetate, their ribosomal proteins were rapidly acetylated within 10 min. Polyacrylamide-urea gel electrophoresis showed that several major ribosomal protein fractions were highly acetylated. By the double-isotope labeling technique, the incorporation of [3H]acetate and [14C]aminoacid mixture into ribosomal proteins and nascent chains was found to be closely associated. Sodium fluoride abolished the acetylation of ribosomal proteins, whereas cycloheximide reduced the acetylation of ribosomal proteins to a much lower level. These findings suggest that acetylation of ribosomal proteins may be involved in the formation of the initiation complex during protein biosynthesis.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=388604Documentos Relacionados
- Biosynthesis of Reticulocyte Membrane Proteins by Membrane-Free Polyribosomes
- PROTEIN SYNTHESIS BY RETICULOCYTE RIBOSOMES, I. INHIBITION OF POLYURIDYLIC ACID-INDUCED RIBOSOMAL PROTEIN SYNTHESIS BY CHLORAMPHENICOL*
- ATP-dependent conjugation of reticulocyte proteins with the polypeptide required for protein degradation.
- Alteration in the Acetylation Level of Ribosomal Protein L12 During Growth Cycle of Escherichia coli
- Protein synthesis by reticulocyte ribosomes. 3. Description of a ribonucleoprotein fraction which stimulates messenger RNA-ribosomal interaction.