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Sentences for "calmodulin "
Like all biochemically characterized unconventional myosins, Myo1c binds calmodulin light chains in its neck region [ 12 ] , this region also interacts with non-calmodulin receptors in hair cells [ 13 ] .
Calmodulin, which can bind up to four Ca 2+ions, generally binds IQ domains in the Ca 2+-free conformation, interaction of Ca 2+-bound calmodulin to other proteins occurs through alternative binding motifs [ 14 ] .
How Ca 2+and calmodulin regulate Myo1c or indeed any myosin-I is unclear.
In conventional myosin, light chains related to calmodulin appear to be essential for stabilization of the myosin lever arm [ 22 ] , a domain that is vital for efficient conversion of chemical energy into mechanical work [ 23 ] .
Calmodulin probably plays a similar lever-arm stabilizing role for Myo1c, Ca 2+-induced calmodulin release would reverse the stabilization and inhibit motility.
To better understand the regulation of Myo1c activity by calmodulin, we sought to more accurately determine how calmodulin binds to Myo1c by measuring the Ca 2+-dependence of calmodulin binding to individual Myo1c IQ peptides.
In addition, to examine the consequences of calmodulin binding to adjacent IQ domains, we measured hydrodynamic properties of recombinant Myo1c-calmodulin complexes, under differing conditions of Ca 2+, calmodulin, and temperature.
Our results indicate that IQ1, IQ2, and IQ3 have calmodulin bound when the concentration of Ca 2+is low, and that increased Ca 2+induces release of calmodulin from IQ1 and IQ2.
Because an excess of unlabeled calmodulin was able to reverse 70-95% of the quench (Fig.
IQ - calmodulin interaction under stoichiometric-titration conditions To determine the affinities of the Myo1c IQ peptides for unlabeled calmodulin, we used Alexa-calmodulin as a reporter (Alexa-calmodulin : unlabeled calmodulin ratio of 1:100) in our binding studies.
5), indicating that, as expected, unlabeled calmodulin binds to the Myo1c IQ peptides.
These experimental conditions resembled a stoichiometric titration, where the total concentration of calmodulin was higher than the K d values for IQ1, IQ2, and IQ3.
Under true stoichiometric-titration conditions (fixed concentration of receptor at 100-fold or more than the K d , varying the ligand concentration up to and beyond the receptor concentration), almost all of the added IQ peptide would bind tightly to calmodulin and linearly decrease the fluorescence, at the point where the IQ-peptide concentration exceeds the calmodulin concentration multiplied by the peptide:calmodulin stoichiometry ( m ), a plateau in the fluorescence intensity would be reached.
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