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J. Biol. Chem., Vol. 264, Issue 12, 6724-6729, 04, 1989
LJ Olsen, SM Theg, BR Selman and K Keegstra
One of the first steps in the transport of nuclear-encoded, cytoplasmically
synthesized precursor proteins into chloroplasts is a specific binding
interaction between precursor proteins and the surface of the organelle.
Although protein translocation into chloroplasts requires ATP hydrolysis,
binding is generally thought to be energy independent. A more detailed
investigation of precursor binding to the surface of chloroplasts showed
that ATP was required for efficient binding. Protein translocation is known
to require relatively high levels (1 mM or more) of ATP. As little as
50-100 microM ATP caused significant stimulation of precursor binding over
controls with no ATP. Several different precursors were tested and all
showed increased binding upon addition of low levels of ATP.
Nonhydrolyzable analogs of ATP did not substitute for ATP, indicating that
ATP hydrolysis was required for binding. A protonmotive force was not
involved in the energy requirement for binding. Other (hydrolyzable)
nucleotides could substitute for ATP but were less effective at stimulating
binding. Binding was stimulated by ATP generated inside chloroplasts even
when an ATP trap was present to destroy external ATP. We conclude that
internal ATP is required for stimulation of precursor binding to
chloroplasts.
ATP is required for the binding of precursor proteins to chloroplasts
Department of Botany, University of Wisconsin, Madison 53706.
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