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Plant Physiol, April 2001, Vol. 125, pp. 2154-2163
Maize Non-Photosynthetic Ferredoxin Precursor Is Mis-Sorted to
the Intermembrane Space of Chloroplasts in the Presence of
Light1
Toshiya
Hirohashi,
Toshiharu
Hase, and
Masato
Nakai*
Institute for Protein Research, Osaka University, 3-2 Yamadaoka,
Suita 565-0871, Japan
Preprotein translocation across the outer and inner envelope
membranes of chloroplasts is an energy-dependent process requiring ATP
hydrolysis. Several precursor proteins analyzed so far have been found
to be imported into isolated chloroplasts equally well in the dark in
the presence of ATP as in the light where ATP is supplied by
photophosphorylation in the chloroplasts themselves. We demonstrate
here that precursors of two maize (Zea mays L. cv Golden
Cross Bantam) ferredoxin isoproteins, pFdI and pFdIII, show distinct
characteristics of import into maize chloroplasts. pFdI, a
photosynthetic ferredoxin precursor, was efficiently imported into the
stroma of isolated maize chloroplasts both in the light and in the
dark. In contrast pFdIII, a non-photosynthetic ferredoxin precursor,
was mostly mis-sorted to the intermembrane space of chloroplastic
envelopes as an unprocessed precursor form in the light but was
efficiently imported into the stroma and processed to its mature form
in the dark. The mis-sorted pFdIII, which accumulated in the
intermembrane space in the light, could not undergo subsequent import
into the stroma in the dark, even in the presence of ATP. However, when
the mis-sorted pFdIII was recovered and used for a separate import
reaction, pFdIII was capable of import into the chloroplasts in the
dark. pFNRII, a ferredoxin-NADP+ reductase isoprotein
precursor, showed import characteristics similar to those of pFdIII.
Moreover, pFdIII exhibited similar import characteristics with
chloroplasts isolated from wheat (Pennisetum americanum)
and pea (Pisum sativum cv Alaska). These findings suggest that the translocation of precursor proteins across the envelope membranes of chloroplasts may involve substrate-dependent light-regulated mechanisms.
1
This work was supported in part by a
Grant-in-Aid for Scientific Research from the Ministry of Education,
Science and Culture of Japan.
*
Corresponding author; e-mail nakai{at}protein.osaka-u.ac.jp; fax
81-6-6879-8613.
© 2001 American Society of Plant Physiologists
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