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THE PLANT CELL, Vol 3, Issue 7 709-717, Copyright © 1991 by American Society of Plant Biologists
Targeting of Proteins to the Outer Envelope Membrane Uses a Different Pathway than Transport into Chloroplasts
Hm. Li, T. Moore and K. Keegstra
Department of Botany, University of Wisconsin, Madison, Wisconsin 53706
The chloroplastic envelope is composed of two membranes, inner and outer,
each with a distinct set of polypeptides. Like proteins in other
chloroplastic compartments, most envelope proteins are synthesized in the
cytosol and post-translationally imported into chloroplasts. Considerable
knowledge has been obtained concerning protein import into most
chloroplastic compartments. However, very little is known about the
biogenesis of envelope membrane proteins. We isolated a cDNA clone from pea
that encodes a 14-kilodalton outer envelope membrane protein. The precursor
form of this protein does not possess a cleavable transit peptide and its
import into isolated chloroplasts does not require either ATP or a
thermolysin-sensitive component on the chloroplastic surface. These
findings, together with similar observations made with a spinach
chloroplastic outer membrane protein, led us to propose that proteins
destined for the outer membrane of the chloroplastic envelope follow an
import pathway distinct from that followed by proteins destined for other
chloroplastic compartments.
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