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Reconstructing the evolutionary history of the artiodactyl ribonuclease
superfamily Thomas M. Jermann, Jochen G. Opitz, Joseph Stackhouse & Steven
A. Benner
Department of Chemistry,
ETH Zürich, CH-8092 Zürich, Switzerland
THE sequences of proteins from ancient organisms can be
reconstructed from the sequences of their descendants by a procedure that
assumes that the descendant proteins arose from the extinct ancestor by the
smallest number of independent evolutionary events
('parsimony')1,2. The reconstructed sequences can
then be prepared in the laboratory and studied3,4. Thirteen
ancient ribonucleases (RNases) have been reconstructed as intermediates in the
evolution of the RNase protein family in artiodactyls (the mammal order that
includes pig, camel, deer, sheep and ox)5. The properties of the
reconstructed proteins suggest that parsimony yields plausible ancient
sequences. Going back in time, a significant change in behaviour, namely a
fivefold increase in catalytic activity against double-stranded RNA, appears in
the RNase reconstructed for the founding ancestor of the artiodactyl lineage,
which lived about 40 million years ago6. This corresponds to the
period when ruminant digestion arose in the artiodactyls, suggests that
contemporary artiodactyl digestive RNases arose from a non-digestive ancestor,
and illustrates how evolutionary reconstructions can help in the understanding
of physiological function within a protein family7–9.
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