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J. Biol. Chem., Vol. 264, Issue 12, 6730-6736, Apr, 1989
SM Theg, C Bauerle, LJ Olsen, BR Selman and K Keegstra
The energy requirements for the import of nuclear-encoded proteins into
isolated chloroplasts have been reinvestigated. We have shown that, in
contrast to protein import into mitochondria, the translocation of the
precursors to ferredoxin, plastocyanin (prPC) and the small subunit of
ribulose-1,5-bisphosphate carboxylase/oxygenase (prSS) across all
chloroplastic membranes is independent of a protonmotive force and requires
only ATP. This extends previous works in which investigations were limited
to prSS and demonstrates that our results are probably general to all
chloroplastic protein precursors. Our results are particularly interesting
for the import of prPC, since in addition to the two envelope membranes,
this protein must traverse the energy- transducing thylakoid membranes en
route to its proper location in the thylakoid lumen. This lack of
involvement of a protonmotive force, specifically of a transmembrane
electric potential, demonstrates that separate mechanisms operate during
the import of proteins into chloroplasts and mitochondria. We also examined
the question of whether ATP is utilized inside or outside of chloroplasts
during protein import. Previous attempts to resolve this question have
resulted in conflicting answers. We found, by two independent approaches,
that ATP for protein import is utilized inside chloroplasts. The
implications of these results on the possible mechanisms of protein import
into chloroplasts are discussed.
Internal ATP is the only energy requirement for the translocation of precursor proteins across chloroplastic membranes
Department of Botany, University of Wisconsin, Madison 53706.
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