Purification and partial characterization of an acidic ribosomal protein kinase from maize
Identifieur interne : 001218 ( Main/Exploration ); précédent : 001217; suivant : 001219Purification and partial characterization of an acidic ribosomal protein kinase from maize
Auteurs : Gabriela Sepúlveda [Mexique] ; Raül Aguilar [Mexique] ; Estela Sánchez De Jiménez [Mexique]Source :
- Physiologia Plantarum [ 0031-9317 ] ; 1995-08.
English descriptors
Abstract
Phosphorylation and dephosphorylation of ribosomal proteins have been suggested to participate in the regulation of protein synthesis in eukaryotic organisms. The present research focuses on the purification and partial characterization of a protein kinase from maize ribosomes that specifically phosphorylates acidic ribosomal proteins. Ribosomes purified from maize axes were used as the enzyme source. Purification of ribosomes was performed by centrifugation through a 0.5 M sucrose, 0.8 M KCl cushion. A protein kinase activity present in this fraction was released by extraction with 1.5 M KCl and further purified by diethylaminoethyl cellulose column chromatography. A peak containing protein kinase activity was eluted around 400 mM KCl. Analysis of this fraction by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis showed one band of 38 kDa molecular mass, which cross‐reacted in a western blot with antibodies raised against proteins from the large ribosomal subunit. This enzyme specifically phosphorylates one of the acidic ribosomal proteins (P2). Its activity is inhibited by Ca2+ and Zn2+ and is activated by Mg2+, polylysine and spermine. The relevance of this protein kinase in reinitiating the protein synthesis process during germination is discussed.
Url:
DOI: 10.1111/j.1399-3054.1995.tb00989.x
Affiliations:
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The present research focuses on the purification and partial characterization of a protein kinase from maize ribosomes that specifically phosphorylates acidic ribosomal proteins. Ribosomes purified from maize axes were used as the enzyme source. Purification of ribosomes was performed by centrifugation through a 0.5 M sucrose, 0.8 M KCl cushion. A protein kinase activity present in this fraction was released by extraction with 1.5 M KCl and further purified by diethylaminoethyl cellulose column chromatography. A peak containing protein kinase activity was eluted around 400 mM KCl. Analysis of this fraction by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis showed one band of 38 kDa molecular mass, which cross‐reacted in a western blot with antibodies raised against proteins from the large ribosomal subunit. This enzyme specifically phosphorylates one of the acidic ribosomal proteins (P2). 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