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The major Euglena thylakoid protein, the light
harvesting chlorophyll a/b-binding protein of photosystem II (pLHCPII)
is synthesized in the cytoplasm as a polyprotein precursor composed of
a 141 amino acid presequence containing a signal peptide domain
followed by eight mature LHCPIIs covalently linked by a decapeptide. To
determine the transport route from cytoplasm to chloroplast and the
site of polyprotein processing, Euglena was pulse labeled with
[
Volume 270,
Number 22,
Issue of June 2, pp. 13084-13090, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
S]sulfate, organelles separated on sucrose
gradients, and pLHCPII and LHCPII immunoprecipitated and separated on
SDS gels. After a 10-min pulse, the pLHCPII polyprotein was found in
the endoplasmic reticulum (ER) and Golgi apparatus. LHCPII was
undetectable after a 10-min pulse consistent with the 20-min half-life
for pLHCPII processing. When pulse-labeled cells were chased for 20 or
40 min with unlabeled sulfate, the fraction of pLHCPII in the ER
decreased, and the fraction in the Golgi apparatus increased. LHCPII
appeared only in thylakoids and chloroplasts, never in the ER or Golgi
apparatus. Na
CO
extraction, a treatment that
releases soluble but not integral membrane proteins, did not remove
pLHCPII from ER and Golgi membranes. Trypsin digestion of ER and Golgi
membranes produced 4 pLHCPII membrane protected fragments. The
Euglena pLHCPII polyprotein is transported as an integral
membrane protein from the ER to the Golgi apparatus and from the Golgi
apparatus to the chloroplast. Polyprotein processing appears to occur
during or soon after chloroplast import of the membrane-bound
precursor.
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