Researchers figure out what makes a simple biological clock tick

the phosphorylation would gradually decrease for 12 hours. However, Johnson and Eglis efforts to purify and crystallize the KaiAC and KaiABC complexes so they could determine their structure using X-ray crystallography repeatedly failed.

It wasnt until they began putting the mixture under the transmission electron microscope that they realized the reason for this failure. "It turns out that the complexes do not form one static structure, which is why we could not crystallize them," says Stewart. "It doesnt go from complex one to complex two three hours later and then three hours later to the next complex. Instead, you have mixtures of all different complexes at all time points, just in different ratios." The researchers divided the 24-hour cycle into seven equal phases: Starting at the lowest level of KaiC phosphorylation, in phases Up1 and Up2 the phosphorylation level increases until it reaches a peak level. Following this "P" phase, the hexamers begin dephosphorylating through phases Down1, Down2 and Down3, reaching its lowest level in the "T" phase (T for trough) and then it starts over.

The analysis also found that, in addition to KaiA, KaiB and KaiC, the test tube also contained large amounts of the three smaller molecules, called monomers, that are the basic building blocks for the bioclock proteins. KaiC is a hexamer that is made up of six monomers. KaiA is a dimer that is made up of two monomers. And KaiB is a tetramer that is made up of four monomers. At the same time that the three proteins are combining into complexes and breaking up again, KaiC is also breaking apart into monomers and then recombining.

While this provided a valuable new insight into the process, it did not explain what was actually going on. To help decipher the dynamics of this system, they turned to Byrne. "The task I was given by Carl was to figure out how this system of three proteins, when combined with ATP, can produce a 24-hour oscillation," says the biomathem

Contact: David F. Salisbury
Vanderbilt University

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