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THE PLANT CELL, Vol 6, Issue 1 93-105, Copyright © 1994 by American Society of Plant Biologists
Envelope Membrane Proteins That Interact with Chloroplastic Precursor Proteins
S. E. Perry and K. Keegstra
Department of Botany, University of Wisconsin, Madison, Wisconsin 53706-1381
The post-translational transport of cytoplasmically synthesized precursor
proteins into chloroplasts requires proteins in the envelope membranes. To
identify some of these proteins, label transfer cross-linking was performed
using precursor to the small subunit of ribulose-1,5-bisphosphate
carboxylase (prSSU) that was blocked at an early stage of the transport
process. Two envelope proteins were identified: an 86-kD protein and a
75-kD protein, both present in the outer membrane. Labeling of both
proteins required prSSU and could not be accomplished with SSU lacking a
transit peptide. Labeling of the 75-kD protein occurred only when low
levels of ATP were present, whereas labeling of the 86-kD protein occurred
in the absence of exogenous ATP. Although both labeled proteins were
identified as proteins of the outer envelope membrane, the labeled form of
the 75-kD protein could only be detected in fractions containing mixed
envelope membranes. Based on these observations, we propose that prSSU
first binds in an ATP-independent fashion to the 86-kD protein. The
energy-requiring step is association with the 75-kD protein and assembly of
a translocation contact site between the inner and outer membrane of the
chloroplastic envelope.
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S. Reinbothe, R. Mache, and C. Reinbothe
A second, substrate-dependent site of protein import into chloroplasts< | |
