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J Biol Chem, Vol. 273, Issue 19, 11405-11408, May 8, 1998
From the Horticultural Sciences Department and Plant Molecular and
Cellular Biology Program, University of Florida, Gainesville, Florida
32611-0690
Signal peptides that specifically direct
precursor proteins to the thylakoid Delta pH pathway possess an N
domain RR motif. Signal peptides that direct transport of bacterial
proteins across a non-Sec export pathway possess an N domain
RRXFLK consensus motif. Recent genetic studies suggest an
evolutionary link between these two protein translocation pathways. To
further explore this relationship, we examined the thylakoid targeting
capability of the signal peptide for Escherichia coli
hydrogenase 1 small subunit (HyaA) by linking it to plastocyanin and
assaying the chimeric protein in an in vitro thylakoid
transport assay. The chimeric precursor was transported across
thylakoids with high efficiency. Transport was characteristic of the
Delta pH but not the Sec pathway, i.e. it was eliminated by
ionophores that dissipate the 
pH but occurred in the absence of
stromal extract or ATP. This result was confirmed by competition with
chemical quantities of a Delta pH pathway precursor. This indicates
that the HyaA signal peptide has the necessary elements for efficient
and exclusive targeting to the Delta pH pathway and further supports
the notion that the alternate targeting pathways in prokaryotes and
plant thylakoids are analogous.
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