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Induction of Acclimative Proteolysis of the Light-Harvesting
Chlorophyll a/b Protein of Photosystem II
in Response to Elevated Light Intensities1
Dan-Hui Yang,
Jeanette Webster2,
Zach Adam,
Marika Lindahl3, and
Bertil Andersson*
Department of Biochemistry, Arrhenius Laboratories for Natural
Sciences, Stockholm University, S-106 91 Stockholm, Sweden (D.-H.Y.,
J.W., M.L., B.A.); and Department of Agricultural Botany, Hebrew
University of Jerusalem, Rehovot 76100, Israel (Z.A.)
Most
plants have the ability to respond to fluctuations in light to minimize
damage to the photosynthetic apparatus. A proteolytic activity has been
discovered that is involved in the degradation of the major
light-harvesting chlorophyll a/b-binding
protein of photosystem II (LHCII) when the antenna size of photosystem II is reduced upon acclimation of plants from low to high light intensities. This ATP-dependent proteolytic activity is of the serine
or cysteine type and is associated with the outer membrane surface of
the stroma-exposed thylakoid regions. The identity of the protease is
not known, but it does not correspond to the recently identified
chloroplast ATP-dependent proteases Clp and FtsH, which are homologs to
bacterial enzymes. The acclimative response shows a delay of 2 d
after transfer of the leaves to high light. This lag period was shown
to be attributed to expression or activation of the responsible
protease. Furthermore, the LHCII degradation was found to be regulated
at the substrate level. The degradation process involves lateral
migration of LHCII from the appressed to the nonappressed thylakoid
regions, which is the location for the responsible protease.
Phosphorylated LHCII was found to be a poor substrate for degradation
in comparison with the unphosphorylated form of the protein. The
relationship between LHCII degradation and other regulatory proteolytic
processes in the thylakoid membrane, such as D1-protein degradation, is discussed.
1
This work was supported by the Swedish Natural
Science Research Council, the Carl Trygger Foundation, and a network
grant from the European Commission Human, Capital, and Mobility program (contract no. ERB CHRX CT 940619).
2
Present address: Department of Medical
Nutrition, Karolinska Institute, Huddinge Hospital, Novum, S-141 86 Huddinge, Sweden.
3
Present address: Department of Agricultural
Botany, Hebrew University of Jerusalem, Rehovot 76100, Israel.
*
Corresponding author; e-mail bertil.andersson{at}biokemi.su.se; fax
46-8-15-36-79.
Plant Physiol. (1998) 118: 827-834
Copyright Clearance Center: 0032-0889/98/118//08
© 1998 American Society of Plant Physiologists
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