Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1998-12-31
|
| pubmed:abstractText |
Muscle-type creatine kinase is known for its unique interaction with the myofibrillar M-band, but the molecular origin for this structural relationship is not well understood. A systematic sequence comparison between the highly homologous cytosolic isoforms, muscle-type and brain-type creatine kinase, yielded two isoenzyme-specific regions in the muscle-type creatine kinases, the M-260 box (residues 258-270) and the M-300 box (residues 300-315). These particular regions were conspicuous for the specific interaction of this CK isoenzyme, but not of brain-type creatine kinase, with the sarcomeric M-band. In situ diffusion assays with fluorescently labeled native, as well as mutated muscle-type creatine kinase variants, were used to study by laser confocal microscopy their association with the M-band of chemically skinned muscle fibers. Neither a set of charge mutants of the M-260 box and/or the M-300 box nor a hybrid construct of both isoforms with the entire C-terminal region derived from the brain-type isoform showed any significant alteration in the in situ M-band-binding properties when compared to the wild-type form of muscle-type creatine kinase. This indicates that in the intact protein of muscle type creatine kinase, these C-terminal isoenzyme-specific regions are not important for M-band interaction and that the actual M-band interaction domain(s) lay mostly within the N-terminal half of the molecule. The highly conserved motives (M-260 box and M-300 box) may serve an isoenzyme-specific purpose yet to be identified.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Sep
|
| pubmed:issn |
0171-9335
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
77
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1-9
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading |
pubmed-meshheading:9808283-Amino Acid Sequence,
pubmed-meshheading:9808283-Animals,
pubmed-meshheading:9808283-Binding Sites,
pubmed-meshheading:9808283-Chickens,
pubmed-meshheading:9808283-Creatine Kinase,
pubmed-meshheading:9808283-Cytosol,
pubmed-meshheading:9808283-Genetic Variation,
pubmed-meshheading:9808283-Isoelectric Focusing,
pubmed-meshheading:9808283-Isoenzymes,
pubmed-meshheading:9808283-Microscopy, Confocal,
pubmed-meshheading:9808283-Molecular Sequence Data,
pubmed-meshheading:9808283-Muscle, Skeletal,
pubmed-meshheading:9808283-Mutagenesis, Site-Directed,
pubmed-meshheading:9808283-Myofibrils,
pubmed-meshheading:9808283-Protein Binding,
pubmed-meshheading:9808283-Protein Conformation,
pubmed-meshheading:9808283-Rats,
pubmed-meshheading:9808283-Sequence Homology, Amino Acid
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
The isoenzyme-diagnostic regions of muscle-type creatine kinase, the M-260 and M-300 box, are not responsible for its binding to the myofibrillar M-band.
|
| pubmed:affiliation |
Swiss Federal Institute of Technology (ETH), Institute of Cell Biology, Zürich.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|