Laboratory resurrection of ancestral proteins has been shown to provide insight into
the ancient properties of biomolecules as well as the intracellular and extracellular
environments hosting these proteins (1-3). Recently, laboratory resurrection efforts
have been reported to successfully target billion years old Precambrian nodes in the
evolution of several proteins (4-6). The characterization of laboratory resurrections
of Precambrian proteins in terms of structure, stability and function will be
described. The biotechnological potential of the extreme properties found for some
resurrected Precambrian proteins (such as hyperstability and enhanced promiscuity)
will be discussed.