Phosphorylation of ribosomal proteins in rabbit reticulocytes. A cell-free system with ribosomal protein kinase activity

David Kabat

Research output: Contribution to journalArticle

56 Citations (Scopus)

Abstract

Rabbit reticulocyte ribosomes isolated from low ionic strength solutions are contaminated with a ribosomal protein kinase. Washing the ribosomes in a high ionic strength solution elutes the kinase. The same ribosomal proteins previously shown to be phosphorylated within reticulocytes incubated with [32P]orthophosphate are labeled in the cell-free system with [γ-32P]ATP. Radioactivity in both cases is incorporated into o-phosphoserine and o-phosphothreonine residues of the polypeptide chains. The rate of ribosomal protein phosphorylation declines as ATP becomes depleted from the cell-free system. The phosphorylation kinetics are accordingly very strongly influenced by ATPase and also by phosphoprotein phosphatase which are present in reticulocytes. The kinase may have a broad substrate specificity since it appears to be active in phosphorylation of chicken erythrocyte histones.

Original languageEnglish (US)
Pages (from-to)197-203
Number of pages7
JournalBiochemistry
Volume10
Issue number2
StatePublished - 1971

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Phosphorylation
Cell-Free System
Ribosomal Proteins
Reticulocytes
Protein Kinases
Rabbits
Ionic strength
Ribosomes
Osmolar Concentration
Phosphotransferases
Adenosine Triphosphate
Phosphothreonine
Phosphoserine
Phosphoprotein Phosphatases
Radioactivity
Substrate Specificity
Washing
Histones
Adenosine Triphosphatases
Chickens

ASJC Scopus subject areas

  • Biochemistry

Cite this

Phosphorylation of ribosomal proteins in rabbit reticulocytes. A cell-free system with ribosomal protein kinase activity. / Kabat, David.

In: Biochemistry, Vol. 10, No. 2, 1971, p. 197-203.

Research output: Contribution to journalArticle

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