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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1981-12-15
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pubmed:abstractText |
1. When etiolated pea seedlings were exposed to continuous light for 24 h and then returned to darkness, 38% of the chlorophyll a, 74% of the chlorophyll b and 84% of the light-harvesting chlorophyll a/b protein that had accumulated under illumination proved to be unstable in darkness. The unstable chlorophyll displayed a half-life of about 90 min. In contrast, alpha and beta subunits of the chloroplast coupling factor and the large and small subunits of ribulose 1,5-biphosphate carboxylase continued to accumulate in darkness, although at a slower rate than in plants maintained under light. 2. Short-term labelling in vivo with L-[35S]methionine showed that leaves continued to synthesize the light-harvesting protein and the small subunit of ribulose 1,5-biphosphate carboxylase for up to 48 h after transfer of plants from light and darkness. However, after long-term labelling (16 h), the light-harvesting chlorophyll a/b protein was found to be labelled to high specific activity only in illuminated leaves. 3. I conclude that the light-harvesting chlorophyll a/b protein is subject to turnover after transfer of plants from light to darkness. The site of breakdown appears to be the photosynthetic membrane. I suggest that turnover of the protein is part of the normal physiological mechanism for co-ordinating the accumulation of the pigment and protein components of the light-harvesting chlorophyll a/b complex.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Chlorophyll,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochromes,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Light-Harvesting Protein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Photosynthetic Reaction Center...,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ribulose-Bisphosphate Carboxylase,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/glutamyl endopeptidase
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
118
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
61-70
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:7026240-Chlorophyll,
pubmed-meshheading:7026240-Cytochromes,
pubmed-meshheading:7026240-Darkness,
pubmed-meshheading:7026240-Endopeptidases,
pubmed-meshheading:7026240-Kinetics,
pubmed-meshheading:7026240-Light,
pubmed-meshheading:7026240-Light-Harvesting Protein Complexes,
pubmed-meshheading:7026240-Photosynthetic Reaction Center Complex Proteins,
pubmed-meshheading:7026240-Plant Proteins,
pubmed-meshheading:7026240-Plants,
pubmed-meshheading:7026240-Ribulose-Bisphosphate Carboxylase,
pubmed-meshheading:7026240-Serine Endopeptidases
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pubmed:year |
1981
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pubmed:articleTitle |
Biosynthesis of the light-harvesting chlorophyll a/b protein. Polypeptide turnover in darkness.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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