A maternal Tubulin promoter drives expression of a fluorescence resonance energy transfer (FRET)-based biosensor for Cdk1 activity. The sqh 3'UTR is also present downstream of the coding sequence. The biosensor is composed of two fluorescent proteins (YPet and mCer) which are separated by sequence comprising a Cdk1 phosphorylation site from cyclin B1 and the polo box domain of Plk1. Phosphorylation of the Cdk1 phosphorylation site results in a conformational change that increases FRET efficiency.