scholarly journals Role of the N-terminal region of the skeletal muscle myosin light chain kinase target sequence in its interaction with calmodulin

1995 ◽  
Vol 4 (11) ◽  
pp. 2375-2382 ◽  
Author(s):  
Wendy A. Findlay ◽  
Michael J. Gradwell ◽  
Peter M. Bayley
Biochemistry ◽  
1983 ◽  
Vol 22 (18) ◽  
pp. 4316-4326 ◽  
Author(s):  
Georg W. Mayr ◽  
Ludwig M. G. Heilmeyer

1989 ◽  
Vol 256 (2) ◽  
pp. C399-C404 ◽  
Author(s):  
B. P. Herring ◽  
M. H. Nunnally ◽  
P. J. Gallagher ◽  
J. T. Stull

A 1.85-kilobase (kb) cDNA has been isolated that encodes the catalytic and calmodulin binding domains of rat skeletal muscle myosin light chain kinase. The cDNA hybridized to a 3.3-kb RNA present in fast- and slow-twitch skeletal muscles. The reported enzymatic activity (3-fold greater in fast- than slow-twitch skeletal muscles) reflects the relative abundance of this RNA in the two types of skeletal muscle. No hybridization of the cDNA was detected to RNA isolated from smooth or nonmuscle tissues. The clone cross hybridized to a 2.2-kb RNA present in cardiac tissue. Ribonuclease protection analysis of skeletal and cardiac muscle RNA revealed major differences in the two hybridizing RNAs. Thus rat skeletal muscle contains a single myosin light chain kinase isoform, which is distinct from the cardiac, smooth, and nonmuscle forms.


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