Phosphorylation of ribosomal proteins influences subunit association and translation of poly (U) in Streptomyces coelicolor

0371869 - MBÚ 2012 RIV GB eng J - Journal Article
Mikulík, Karel - Bobek, Jan - Ziková, Alice - Smětáková, Magdalena - Bezoušková, Silvia
Phosphorylation of ribosomal proteins influences subunit association and translation of poly (U) in Streptomyces coelicolor.
Molecular BioSystems. Roč. 7, č. 3 (2011), s. 817-823. ISSN 1742-206X
R&D Projects: GA ČR GAP302/10/0468; GA ČR GA303/09/0475; GA ČR GA310/07/1009; GA AV ČR(CZ) IAA500110805
Institutional research plan: CEZ:AV0Z50200510
Keywords : ESCHERICHIA-COLI RIBOSOME * ELONGATION-FACTOR-G * MESSENGER-RNA
Subject RIV: EE - Microbiology, Virology
Impact factor: 3.534, year: 2011

The occurrence of phosphorylated proteins in ribosomes of Streptomyces coelicolor was investigated. Little is known about which biological functions these posttranslational modifications might fulfil. A protein kinase associated with ribosomes phosphorylated six ribosomal proteins of the small subunit (S3, S4, S12, S13, S14 and S18) and seven ribosomal proteins of the large subunit (L2, L3, L7/L12, L16, L17, L23 and L27). The ribosomal proteins were phosphorylated mainly on the Ser/Thr residues. Phosphorylation of the ribosomal proteins influences ribosomal subunits association. Ribosomes with phosphorylated proteins were used to examine poly (U) translation activity. Phosphorylation induced about 50 percent decrease in polyphenylalanine synthesis
Permanent Link: http://hdl.handle.net/11104/0205288