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Plant Physiol, January 2000, Vol. 122, pp. 235-242
Interaction of a Plant 14-3-3 Protein with the Signal Peptide of
a Thylakoid-Targeted Chloroplast Precursor Protein and the Presence of
14-3-3 Isoforms in the Chloroplast Stroma1
Paul C.
Sehnke,
Ralph
Henry,2
Kenneth
Cline, and
Robert J.
Ferl*
Program in Plant Molecular and Cellular Biology, Department of
Horticultural Sciences, University of Florida, Gainesville, Florida
32611.
The
14-3-3 proteins are acidic, dimeric proteins that have been implicated
in many eukaryotic cellular processes because of direct protein
association with enzymes and other metabolic and regulatory proteins.
14-3-3 proteins are largely considered to be cytoplasmic, but a search
for proteins that specifically interact with a plant 14-3-3 resulted in
the isolation of a nuclear-encoded, thylakoid-targeted chloroplast
precursor, the full-length Arabidopsis photosystem I N-subunit At
pPSI-N (P.C. Sehnke, R.J. Ferl [1995] Plant Physiol 109: 1126). Using
precursor truncations in the two-hybrid system, it was determined that
the leader sequence is the site of PSI-N that associates with 14-3-3. This suggested the novel possibility that 14-3-3 would be found within
chloroplasts. Immuno-electron microscopy of leaf tissue and western
analysis of chloroplast fractions with monoclonal anti-14-3-3
antibodies localized 14-3-3 proteins to the chloroplast stroma and the
stromal side of thylakoid membranes. Using peptide-generated,
isoform-specific antibodies, GF14 , GF14 , GF14µ, and GF14
were shown to be present in the chloroplast stromal extract. These
isoforms represent two distinct phylogenetic 14-3-3 groupings. These
data suggest a novel interorganellar role for these phylogenetically
distinct 14-3-3 proteins.
1
This work was supported by a grant from the U.S.
Department of Agriculture, National Research Initiative (grant
no. 97-35304-4942). This article is Florida Agricultural Experiment
Station Journal Series No. R-07231.
2
Present address: University of Arkansas,
Department of Biological Sciences, Fayetteville, AK 72701.
*
Corresponding author; e-mail robferl{at}ufl.edu; fax 352-392-1928.
© 2000 American Society of Plant Physiologists
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