Cross talk between protein kinase CK2 and eukaryotic translation initiation factor eIF2beta subunit
| Autor: | Llorens, F, Sarno, Stefania, Sarró, E, Duarri, A, Roher, N, Meggio, Flavio, Plana, M, Pinna, Lorenzo, Itarte, E. |
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| Rok vydání: | 2005 |
| Předmět: |
enzymic regulation
Amino Acid Motifs Eukaryotic Initiation Factor-2 Catalysis protein phosphorylation Substrate Specificity eIF2 protein kinase CK2 surface plasmon resonance protein interaction Protein Subunits Catalytic Domain Mutation Animals Humans Phosphorylation Casein Kinase II Holoenzymes Oligopeptides Protein Binding |
| Zdroj: | Molecular and cellular biochemistry. 274(1-2) |
| ISSN: | 0300-8177 |
| Popis: | The beta-subunit of eukaryotic translation initiation factor eIF2 is a substrate and a partner for protein kinase CK2. Surface plasmon resonance analysis shows that the truncated form corresponding to residues 138-333 of eIF2beta (eIF2beta-CT) interacts with CK2beta as efficiently as full length eIF2beta, whereas the form corresponding to residues 1-137, which contains the CK2 phosphorylation sites, (eIF2beta-NT) does not bind. The use of different mutants and truncated forms of CK2alpha allowed us to map the basic segment K74-K83 at the beginning of helix alphaC and residues R191R195K198 in the p + 1 loop as the main determinants for the binding to eIF2beta-CT of either the isolated CK2alpha subunit or the CK2 holoenzyme. The presence of eIF2beta-CT stimulated the activity of CK2alpha towards the RRRAADSDDDDD peptide substrate; effect that was not observed with the CK2a K74-77A whose ability to bind to eIF2beta-CT is severely impaired. Gel filtration analysis confirmed the ability of CK2alpha to form complexes with eIF2beta-CT, and the contribution of the basic cluster in CK2alpha (K74-K77) in this association. |
| Databáze: | OpenAIRE |
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