Drosophila protein kinase CK2 is rendered temperature-sensitive by mutations of highly conserved residues flanking the activation segment
| Autor: | Ezgi Kunttas-Tatli, Pallavi P. Kuntamalla, Umesh C. Karandikar, Clifton P. Bishop, Ashok P. Bidwai |
|---|---|
| Rok vydání: | 2008 |
| Předmět: |
Models
Molecular Protein Conformation Molecular Sequence Data Clinical Biochemistry Sequence alignment medicine.disease_cause Article Mice Protein structure medicine Animals Drosophila Proteins Humans Amino Acid Sequence Casein Kinase II Protein kinase A Molecular Biology Genetics Mutation biology Temperature Cell Biology General Medicine biology.organism_classification Null allele Enzyme Activation Drosophila melanogaster Casein kinase 2 Sequence Alignment Drosophila Protein |
| Zdroj: | Molecular and Cellular Biochemistry. 323:49-60 |
| ISSN: | 1573-4919 0300-8177 |
| DOI: | 10.1007/s11010-008-9963-6 |
| Popis: | CK2 is a Ser/Thr protein kinase essential for animal development. Although null alleles for CK2 are available in the mouse and Drosophila models, they are lethal when homozygous, thus necessitating conditional alleles for analysis of its developmental roles. We describe the isolation of temperature-sensitive (ts) alleles of Drosophila CK2alpha (dCK2alpha). These alleles efficiently rescue lethality of yeast lacking endogenous CK2 at 29 degrees C, but this ability is lost at higher temperatures in an allele-specific manner. These ts-variants exhibit properties akin to the wild type protein, and interact robustly with dCK2beta. Modeling of these ts-variants using the crystal structure of human CK2alpha indicates that the affected residues are in close proximity to the active site. We find that substitution of Asp(212) elicits potent ts-behavior, an important finding because this residue contributes to stability of the activation segment and is invariant in other Ser/Thr protein kinases. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full text from SpringerLink