Biochemical properties of chimeric skeletal and smooth muscle myosin light chain kinases

Sancy A. Leachman, Patricia J. Gallagher, B. Paul Herring, Michael J. McPhaul, James T. Stull

Research output: Contribution to journalArticlepeer-review

31 Scopus citations

Abstract

The molecular and biochemical properties of myosin light chain kinases from chicken skeletal and smooth muscle were investigated by recombinant DNA techniques. Deletion of the amino-terminal region of either the smooth or skeletal muscle myosin light chain kinase resulted in a decrease in Vmax with no significant change in Km, values for light chain substrates. Skeletal/smooth muscle chimeric kinases were inactive when a 65-residue region amino-terminal of the catalytic core was exchanged between the two forms. Changing alanine 494 to glutamic acid within this region in the chicken skeletal muscle myosin light chain kinase increased the Km values for light chains 10-fold. These results are consistent with the hypothesis that the region amino-terminal of the catalytic core in myosin light chain kinases is involved in light chain recognition. A skeletal muscle kinase which contained the smooth muscle calmodulin binding domain remained regulated by Ca2+/calmodulin. Thus, the calmodulin binding domains of smooth and skeletal muscle myosin light chain kinases share structural elements necessary for regulation.

Original languageEnglish (US)
Pages (from-to)4930-4938
Number of pages9
JournalJournal of Biological Chemistry
Volume267
Issue number7
StatePublished - Mar 5 1992
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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