Molecular characterization of rat skeletal muscle myosin light chain kinase

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...

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Published inThe American journal of physiology Vol. 256; no. 2 Pt 1; p. C399
Main Authors Herring, B P, Nunnally, M H, Gallagher, P J, Stull, J T
Format Journal Article
LanguageEnglish
Published United States 01.02.1989
Subjects
Amino Acid Sequence
Animals
Base Sequence
Blotting, Northern
Cloning, Molecular
DNA, Recombinant - metabolism
Genes
Molecular Sequence Data
Muscles - enzymology
Myosin-Light-Chain Kinase - genetics
Oligonucleotide Probes
Rats
RNA - genetics
RNA, Antisense
RNA, Messenger - antagonists & inhibitors
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Summary: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.
ISSN:0002-9513
2163-5773
DOI:10.1152/ajpcell.1989.256.2.C399