Interaction of casein kinase II with ribosomal protein L22 of Drosophila melanogaster

Biochem Biophys Res Commun. 2002 Oct 18;298(1):60-6. doi: 10.1016/s0006-291x(02)02396-3.

Abstract

The ubiquitous eukaryotic protein kinase CKII (casein kinase II) has been found to interact with a number of cellular proteins, either through the catalytic subunit or the regulatory subunit. Using the yeast two-hybrid screening method, we found that the catalytic subunit of Drosophila melanogaster CKII (DmCKII) interacts with Drosophila ribosomal protein L22 (rpL22). This interaction was also observed in vitro with a glutathione-S-transferase (GST)-rpL22 fusion protein. The predicted full-length Drosophila rpL22 protein has an N-terminal extension rich in alanine, lysine, and proline that appears to be unique to Drosophila. Deletion mapping revealed that the conserved core of rpL22 is responsible for the interaction with CKII. Moreover, purified DmCKII can phosphorylate a GST-L22 fusion protein at the C-terminal end, suggesting that this protein may be a substrate of CKII in Drosophila.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Casein Kinase II
  • Drosophila Proteins*
  • Drosophila melanogaster / enzymology*
  • Drosophila melanogaster / metabolism
  • Molecular Sequence Data
  • Phosphorylation
  • Protein Serine-Threonine Kinases / metabolism*
  • RNA-Binding Proteins / chemistry
  • RNA-Binding Proteins / genetics
  • RNA-Binding Proteins / metabolism*
  • Ribosomal Proteins*
  • Two-Hybrid System Techniques

Substances

  • Drosophila Proteins
  • RNA-Binding Proteins
  • Ribosomal Proteins
  • RpL22 protein, Drosophila
  • Casein Kinase II
  • Protein Serine-Threonine Kinases

Associated data

  • GENBANK/U42587