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J. Biol. Chem., Vol. 269, Issue 40, 24723-24727, 10, 1994
G Zhi, BP Herring and JT Stull
Site-directed and chimeric mutations of myosin regulatory light chains were
used to identify residues important for phosphorylation of Ser19 by smooth
muscle myosin light chain kinase. Arg16 and hydrophobic residues C-terminal
of Ser19 in smooth muscle light chain were important substrate determinants
in the intact protein. However, changes in the kinetic properties with
mutations in the light chain were substantially smaller than results
reported with structurally similar synthetic peptide substrates. These
results together with the low Vmax value for short peptide substrates
containing the consensus phosphorylation sequence suggest that there may be
additional sites of interactions between the kinase and protein substrate.
Chimeras of skeletal and smooth muscle light chains were constructed with
exchanges at the N terminus and subdomains I, II, III, and IV. Analysis of
results obtained on the kinetic properties for phosphorylation showed that
subdomains I and II contribute to high Vmax values. Thus, a region distant
from the consensus phosphorylation sequence in smooth muscle light chain is
also an important substrate determinant for myosin light chain kinase.
Structural requirements for phosphorylation of myosin regulatory light chain from smooth muscle
Department of Physiology, University of Texas Southwestern Medical Center at Dallas 75235-9040.
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