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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1995-6-27
|
| pubmed:abstractText |
Casein kinase II, cyclin-dependent kinases, and glycogen synthase kinase-3 are members of the protein kinase subfamily with a prominent insert in domain X of their catalytic subunit sequence. The function of the insert sequence in casein kinase II was investigated utilising synthetic peptides corresponding to the insert, cross-linking experiments, and the generation of casein kinase II insert region mutants. The mutation of basic residues (R276-->A, R278-->A, R281-->A, K277-->A) within the major insert sequence (PRFHDILQRHSRKRWERFVHSDNQHL, positions 265-290) did not affect alpha/beta subunit association, enzyme tetramerisation, thermal stability, and peptide (RRRDDDSDDD-NH2) phosphorylation. Similarly, replacement of residues 276-290 within the major insert with the corresponding residues from the cell-cycle kinase cyclin-dependent kinase 2 (CDK2) (FPKWKPGSLASHVKN) had no significant effect. The mutation of charged residues (H232-->A, H234-->A, D235-->A) within a nearby minor insert sequence (HGHDNY, positions 232-237), or replacement of residues 234-237 with the corresponding residues from CDK2 (DSEI) also did not affect alpha/beta subunit association and tetramerisation, but reduced enzyme thermal stability to more closely resemble the stability of the isolated alpha-subunit. In addition, mutations within the minor insert caused approximately a threefold increase in the apparent Km for peptide substrate. The results indicate that the major and minor inserts are not essential for alpha/beta subunit association, but the minor insert region influences substrate binding and thermal stability.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CDC2 Protein Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Casein Kinase II,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
May
|
| pubmed:issn |
0014-2956
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
1
|
| pubmed:volume |
229
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
703-9
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:7758466-Amino Acid Sequence,
pubmed-meshheading:7758466-Animals,
pubmed-meshheading:7758466-Binding Sites,
pubmed-meshheading:7758466-CDC2 Protein Kinase,
pubmed-meshheading:7758466-Casein Kinase II,
pubmed-meshheading:7758466-Cattle,
pubmed-meshheading:7758466-DNA-Binding Proteins,
pubmed-meshheading:7758466-Drosophila melanogaster,
pubmed-meshheading:7758466-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:7758466-Male,
pubmed-meshheading:7758466-Molecular Sequence Data,
pubmed-meshheading:7758466-Mutagenesis, Insertional,
pubmed-meshheading:7758466-Peptide Fragments,
pubmed-meshheading:7758466-Plasmids,
pubmed-meshheading:7758466-Protein-Serine-Threonine Kinases,
pubmed-meshheading:7758466-Rabbits,
pubmed-meshheading:7758466-Structure-Activity Relationship,
pubmed-meshheading:7758466-Testis
|
| pubmed:year |
1995
|
| pubmed:articleTitle |
Insert regions in domain X of the casein kinase II catalytic subunit.
|
| pubmed:affiliation |
St. Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|