The signal recognition particle (SRP) and its membrane-associated receptor
(SR) catalyze targeting of nascent secretory and membrane proteins to the p
rotein translocation apparatus of the cell. Components of the SRP pathway a
nd salient features of the molecular mechanism of SRP-dependent protein tar
geting are conserved in all three kingdoms of life. Recent advances in the
structure determination of a number of key components in the eukaryotic and
prokaryotic SRP pathway provide new insight into the molecular basis of SR
P function, and they set the stage for future work toward an integrated pic
ture that takes into account the dynamic and contextual properties of this
remarkable cellular machine.