The eukaryotic acid ribosomal P0, P1, and P2 proteins share a conserved flexible C-terminal tail that is rich in acidic residues, which are involved in the interaction with elongation factor 2 during protein synthesis. Our previous work suggested that the acidic ribosomal P proteins
from Euplotes octocarinatus have a special C-terminal domain. To further understand this characteristic feature, both P2 and elongation factor 2 from E.
octocarinatus were overexpressed, for the first time, in Escherichia coli in this study. GST pull-down assay
indicated that P2 protein from E.
octocarinatus (EoP2) interacted specifically with the N-terminal domain of elongation factor 2 from E.
octocarinatus (EoEF-2) in vitro. The interacting part of EoP2 is in the C-terminal domains, consistent with the observation in
other organisms. Phosphorylation of the recombinant EoP2 was performed in vitro using multiple methods such as 31P-NMR spectroscopy, native PAGE, and Phos-tagTM SDS-PAGE. Results showed that ribosomal protein EoP2 was phosphorylated by casein kinase II at serine 21 located
at the N terminus. This phosphorylation site identified in EoP2 is quite different from that of P2 from other organisms, in which the phosphorylation site is located in the conserved C-terminal region.
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acidic ribosomal protein;
protéine ribosimique acide
Document Type: Research Article
Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education, Institute of Biotechnology, Shanxi University, Taiyuan 030006, China.
Research Institute of Applied Chemistry, Shanxi University, Taiyuan 030006, China.
Institute of Molecular Science, Shanxi University, Taiyuan 030006, China.
Publication date: January 1, 2014
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