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J. Biol. Chem., Vol. 269, Issue 23, 16148-16154, Jun, 1994
A Persechini, K McMillan and P Leakey
We have investigated the abilities of calmodulin (CaM) tryptic fragments
1-75 (TRCI) or 78-148 (TRCII) to activate gizzard smooth muscle myosin
light chain kinase (gMLCK), rabbit skeletal muscle myosin light chain
kinase (skMLCK), and neural nitric oxide synthase (nNOS) activities. Our
results indicate for all three enzymes that binding of CaM follows an
ordered mechanism wherein the C-terminal lobe, represented by TRCII, binds
specifically to a site we designated as A, followed by binding of the
N-terminal lobe, represented by TRCI, to a site designated as B. With TRCII
and TRCI bound to their respective sites, skMLCK and gMLCK activities are
both activated to about 80% of their maximum levels. Occupancy of both
sites in the MLCK enzymes by TRCI results in only low levels of enzyme
activation; occupancy of both sites by TRCII also results in low levels of
gMLCK activity, but activates skMLCK activity to 65% of the maximum level.
With TRCI bound at site B and either TRCII or TRCI bound at site A, nNOS
activity is 50% of the maximum level. Apparent dissociation constants for
TRCII binding to site A and TRCI binding to site B are, respectively; 0.3
and 3 microM (skMLCK); 1.2 and 0.8 microM (gMLCK); 10 nM and 150 microM
(nNOS). Our results demonstrate that the CaM lobes can make distinct
contributions to binding and/or activation of different CaM-dependent
enzymes and that the tethering function of the central helix can be
mimicked by sufficiently high concentrations of the CaM fragments. We have
modeled tethering as if it stabilizes the CaM-enzyme complex by creating a
high effective concentration of the N-terminal lobe. Calculated values for
this concentration term indicate essentially identical contributions by the
central helix to the observed nanomolar dissociation constants of the three
CaM-enzyme complexes examined.
Activation of myosin light chain kinase and nitric oxide synthase activities by calmodulin fragments
Department of Physiology, University of Rochester Medical Center, New York 14642.
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