| Induction of acclimative proteolysis of the light-harvesting chlorophyll a/b protein of photosystem II in response to elevated light intensities | |
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MedLine Citation:
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PMID: 9808726 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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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. |
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Authors:
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Yang; Webster; Adam; Lindahl; Andersson |
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Publication Detail:
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Type: JOURNAL ARTICLE |
Journal Detail:
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Title: Plant physiology Volume: 118 ISSN: 1532-2548 ISO Abbreviation: Plant Physiol. Publication Date: 1998 Nov |
Date Detail:
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Created Date: 1998-11-26 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0401224 Medline TA: Plant Physiol Country: - |
Other Details:
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Languages: Eng Pagination: 827-34 Citation Subset: - |
Affiliation:
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Department of Biochemistry, Arrhenius Laboratories for Natural Sciences, Stockholm University, S-106 91 Stockholm, Sweden (D.-H.Y., J.W., M.L., B.A.). |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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