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Cameleon (protein)

Engineered protein used to visualize calcium levels in living cells

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Through Calcium

Mechanism

The DNA encoding cameleon fusion protein must be either stably or transiently introduced into the cell of interest. Protein made by the cell according to this DNA information then serves as a fluorescent indicator of calcium concentration. In the presence of calcium, Ca2+ binds to M13, which enables calmodulin to wrap around the M13 domain. This brings the two GFP-variant proteins closer to each other, which increases FRET efficiency between them. A time-resolved spectroscopy study done on resonance energy transfer by Habuchi et al. in 2002 suggested the existence of 3 different calmodulin conformations that were dependent on Ca2+ binding. The study concluded that the mechanism of conformation interconversion remains unclear, but the data provided estimates of rate constants, energy transfer efficiency, and donor-acceptor distances in Ca2+-free and Ca2+-bound YC3.1 cameleon proteins.

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