منابع مشابه
Acetylation of ribosomal proteins. I. Characterization and properties of rat liver ribosomal proteins.
Rat liver ribosomes have been acetylated both in vivo and in vitro. The in vivo acetylation of ribosomes occurred within 5 min of the administration of t3H]acetate, and 70 to 80% of the incorporated radioactivity remained in the ribosomal proteins after removal of RNA with urea-LiCl. Following treatment of the acetylated ribosomai proteins with ethanol-ether, RNase, and 0.5 M KCl, to remove pos...
متن کاملAcetylation of reticulocyte ribosomal proteins at time of protein biosynthesis.
When rabbit reticulocytes were incubated in vitro with [(3)H]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 [(3)H]acetate and [(14)C]aminoacid mixture into ribosomal proteins and nascent cha...
متن کاملAcetylation of Ribosomal Proteins in Regenerating Rat Liver
It has been shown that rat liver ribosomal proteins can be acetylated both in viuo and in vitro (Liew & Gornall, 1973). After purification of the ribosomal proteins to remove any possible contamination by lipids, nucleotides and cytoplasmic protein, the radioactivity still remained in these proteins. When the [’Hlacetate-labelled ribosomal proteins were hydrolysed in strong acid at 110°C overni...
متن کاملN(α)-Acetylation of yeast ribosomal proteins and its effect on protein synthesis.
N(α)-Acetyltransferases (NATs) cause the N(α)-acetylation of the majority of eukaryotic proteins during their translation, although the functions of this modification have been largely unexplored. In yeast (Saccharomyces cerevisiae), four NATs have been identified: NatA, NatB, NatC, and NatD. In this study, the N(α)-acetylation status of ribosomal protein was analyzed using NAT mutants combined...
متن کاملModification of Yeast Ribosomal Proteins
Two-dimensional polyacrylamide-gel electrophoretic analysis of yeast ribosomal proteins uniformly labelled in vivo with [methyl-3H]methionine and [1-'4C]methionine revealed that four ribosomal proteins are methylated, i.e. proteins S31, S32, L15 and L41. Lysine and arginine appear to be the predominant acceptors of the methyl groups. The degree of methylation ranges from 0.09 to 0.20 methyl gro...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1973
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)44360-3