The BioGRID | PUBLICATION VIEW

	Biochem. Biophys. Res. Commun. Sep (1999); 263(2):475-81
Phosphorylation of ribosomal protein L5 by protein kinase CKII decreases its 5S rRNA binding activity.
Park JW, Bae YS
College of Natural Sciences, Kyungpook National University, Taegu, 702-701, Korea.
Abstract: We have recently reported that ribosomal protein L5 associates with the beta subunit of protein kinase CKII (CKII) (Kim, J.-M., Cha, J. -Y., Marshak, D. R., and Bae, Y.-S. (1996) Biochem. Biophys. Res. Commun. 226, 180-186). In this study, we demonstrate that CKII is able to catalyze the phosphorylation of the human L5 protein in vitro, which results in a decrease in 5S rRNA binding activity. Phosphoamino acid analysis indicated that the phosphorylation occurs on serine residues. Sequence analysis of cyanogen bromide-digested phosphopeptides and analysis of L5 deletion mutants indicates that the main phosphorylated residues are located within two fragments corresponding of residues 142-200 and residues 272-297 of the human L5. Based on our present results, we suggest that the phosphorylation of L5 by CKII is one of the mechanisms that regulates nucleolar targeting of 5S rRNA and/or ribosome assembly in the cell.
[PUBMED: 10491318]