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Plant Physiol, August 2000, Vol. 123, pp. 1525-1536
Dephosphorylation of Photosystem II Reaction Center Proteins in
Plant Photosynthetic Membranes as an Immediate Response to Abrupt
Elevation of Temperature1
Anne
Rokka,
Eva-Mari
Aro,
Reinhold G.
Herrmann,
Bertil
Andersson, and
Alexander V.
Vener2*
Department of Biochemistry, Arrhenius Laboratories for Natural
Sciences, Stockholm University, S-106 91 Stockholm, Sweden (A.R.,
B.A., A.V.V); Department of Biology, University of Turku, FIN-20014,
Turku, Finland (A.R., E-M.A); Botanisches Institut der
Ludwig-Maximilians-Universität, Menzinger Strasse 67, D-80638 München, Germany (R.G.H.); and Division of Cell Biology,
Linköping University, S-581 85 Linköping, Sweden
(B.A.)
Kinetic studies of protein dephosphorylation in photosynthetic
thylakoid membranes revealed specifically accelerated dephosphorylation of photosystem II (PSII) core proteins at elevated temperatures. Raising the temperature from 22°C to 42°C resulted in a more than 10-fold increase in the dephosphorylation rates of the PSII reaction center proteins D1 and D2 and of the chlorophyll a
binding protein CP43 in isolated spinach (Spinacia
oleracea) thylakoids. In contrast the dephosphorylation rates
of the light harvesting protein complex and the 9-kD protein of the
PSII (PsbH) were accelerated only 2- to 3-fold. The use of a
phospho-threonine antibody to measure in vivo phosphorylation levels in
spinach leaves revealed a more than 20-fold acceleration in D1, D2, and
CP43 dephosphorylation induced by abrupt elevation of temperature, but
no increase in light harvesting protein complex dephosphorylation. This
rapid dephosphorylation is catalyzed by a PSII-specific, intrinsic
membrane protein phosphatase. Phosphatase assays, using intact
thylakoids, solubilized membranes, and the isolated enzyme, revealed
that the temperature-induced lateral migration of PSII to the
stroma-exposed thylakoids only partially contributed to the rapid
increase in the dephosphorylation rate. Significant activation of the
phosphatase coincided with the temperature-induced release of TLP40
from the membrane into thylakoid lumen. TLP40 is a peptidyl-prolyl
cis-trans isomerase, which acts as a regulatory subunit of the membrane phosphatase. Thus dissociation of TLP40 caused by an abrupt elevation in temperature and activation of the membrane protein phosphatase are
suggested to trigger accelerated repair of photodamaged PSII and to
operate as possible early signals initiating other heat shock responses
in chloroplasts.
1
Support for this work was provided by the
Swedish Natural Science Research Council, by The Academy of Finland, by
the Swedish Council for Forestry and Agricultural Research, by Nordiskt
Kontaktorgan för Jordbruksforskning, by The Nordic Energy
Research Program, by The German Research Foundation (SFB 184), and by
the Human Frontier Science Program.
2
Present address: Department of Horticulture, University
of Wisconsin, Madison, WI 53706.
*
Corresponding author; e-mail avvener{at}facstaff.wisc.edu; fax
608-262-47-43.
© 2000 American Society of Plant Physiologists
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