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Volume 270,
Number 43,
Issue of October 27, 1995 pp. 25685-25695
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
In Vitro Synthesis and Assembly of Photosystem II Core Proteins
THE D1 PROTEIN CAN BE INCORPORATED INTO PHOTOSYSTEM II IN ISOLATED
CHLOROPLASTS AND THYLAKOIDS
(Received for publication, June 20, 1995; and in revised form, August 9, 1995)
Klaas J.
van
Wijk
, ,
Sophie
Bingsmark
,
Eva-Mari
Aro
,
Bertil
Andersson
The D1 reaction center protein of the membrane-bound photosystem
II complex (PSII) has a much higher turnover rate than the other PSII
proteins. Thus, the D1 protein has to be replaced while the other PSII
components are not newly synthesized. In this study, this D1 protein
replacement into PSII complexes was followed in two in vitro translation systems: isolated chloroplasts and a homologous
run-off translation system consisting primarily of isolated thylakoids
with attached ribosomes. The incorporation of newly synthesized
radiolabeled products into different (sub)complexes was analyzed by
sucrose density gradient centrifugation of n-dodecyl
-D-maltoside-solubilized thylakoid membranes. This
analysis allowed us to follow the release of the nascent polypeptide
chains from the ribosomes and identification of at least four assembly
steps of the PSII complex, as shown below. (i) Both in isolated
chloroplasts and in thylakoids, newly synthesized D1 protein is
predominantly incorporated into existing PSII subcomplexes, indicating
that synthesis and import of nuclear-encoded factors is not needed for
D1 protein replacement. (ii) In chloroplasts, D1 protein
incorporation into PSII core complexes is more efficient than during
translation in isolated thylakoids. In the thylakoid translation
system, a large percentage of radiolabeled D1 protein is found in
smaller PSII subcomplexes, like PSII reaction center particles, and as
unassembled protein in the membrane. This indicates that stromal
factors are required in the replacement process of the D1 protein. (iii) Both in isolated chloroplasts and in thylakoids, the other
PSII core proteins D2, CP43, and CP47 are also synthesized and released
from the membrane-bound ribosomes, but incorporation into PSII
complexes occurs to a much smaller extent than the D1 protein. Instead
they accumulate predominantly as unassembled proteins in the thylakoid
membrane. (iv) In chloroplasts, synthesis of the D1 protein seems to
be adjusted according to the possibilities of incorporation into PSII
complexes, while synthesis of the D2 protein, CP43, and CP47 is less
regulated and their accumulation as unassembled protein in the membrane
is abundant.

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Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.
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