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The Journal of Biochemistry
Year: 2009  |  Volume: 146  |  Issue: 4  |  Page No.: 581 - 590

Photocontrol of Calmodulin Interaction with Target Peptides using Azobenzene Derivative

H Shishido, M. D Yamada, K Kondo and S. Maruta    

Abstract:

Calmodulin (CaM), a physiologically important Ca2+-binding protein, participates in numerous cellular regulatory processes. It is dumbbell shaped and contains two globular domains connected by a short -helix. Each of the globular domains has two Ca2+-binding sites, the EF hands. CaM undergoes a conformational change upon binding to Ca2+, which enables it to bind to specific proteins for specific responses. Here, we successfully photocontrolled CaM binding to its target peptide using the photochromic compound N-(4-phenylazophenyl) maleimide (PAM), which reversibly undergoes cis–trans isomerization upon ultraviolet (UV) and visible (VIS) light irradiation. In order to specifically incorporate PAM, CaM mutants having reactive cysteine residues in the functional region were prepared; PAM was stoichiometrically incorporated into the cysteine residues in these mutants. Further, we prepared the target peptide, M13, fused with yellow fluorescent protein (YFP) to monitor the CaMM13 peptide interaction. The binding of the PAMCaM mutants, N60C, D64C and M124C, to M13YFP was reversibly photocontrolled upon UVVIS light irradiation at appropriate Ca2+ concentrations.

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