We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Mapping of the Interaction Domain of the Protein Kinase CKII β Subunit with Target Proteins.
- Authors
Bong-Hyun Ahn; Tae-Hyun Kim; Young-Seuk Bae
- Abstract
Protein kinase CKII is composed of two catalytic (α or α′) subunits and two regulatory (β) subunits. The CKIIβ subunit is thought to mediate the tetramer formation and interact with other target proteins. Previously we have shown that CKIIβ interacts with ribosomal proteins L5 and L41, DNA topoisomerase IIβ, and SAG/CKBBP∼. In this study, the two-hybrid system was used to define the subregions of CKIIβ that are involved in the interaction with L5, L41, topoisomerase IIβ̣, SAG/CKBBP1, and unknown proteins, CKBBP2 and CKBBP3. The results indicated that the region between residues 1 and 167 of CKIIβ is common binding site for L5, topoisomerase IIβ, SAG/ CKBBP1, and L41. The region between amino acids 19 and 167 of CKIIβ is sufficient for the interaction with CKBBP3. The region between residues 67 and 130 of CKIIβ is a minimal fragment that is required for interaction with CKBBP2. Overlay experiments showed that the region between residues 1 and 167 of CKIIβ interacts with L5, L41, and SAG/CKBBP1 in vitro. These results suggest that the binding sites of CKIIβ for these target proteins are not located within a small linear sequence stretch, but rather are created by a three-dimensional structure.
- Subjects
PROTEIN kinase CK2; PROTEIN kinases; PHOSPHOTRANSFERASES; PROTEINS; AMINO acids
- Publication
Molecules & Cells (Springer Nature), 2001, Vol 12, Issue 2, p158
- ISSN
1016-8478
- Publication type
Article
- DOI
10.1016/s1016-8478(23)17077-4