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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1983-11-23
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pubmed:abstractText |
The effect of protein phosphorylation on the distribution of chlorophyll-protein complexes between appressed and non-appressed thylakoid regions of spinach chloroplasts has been investigated. Stroma lamellae vesicles and inside-out vesicles, representative of non-appressed and appressed thylakoids, respectively, were isolated from thylakoid membranes before and after phosphorylation. The fractions were analyzed with respect to the yield of vesicles, incorporation of [32P]phosphate into the light-harvesting chlorophyll-a/b--protein complex, chlorophyll composition, and the relative content of the main chlorophyll-protein complexes. The yield of inside-out vesicles from phosphorylated thylakoids was 20% lower than that from control thylakoids, indicating a partial destacking. The specific incorporation of [32P]phosphate into the light-harvesting chlorophyll-a/b--protein complex was at least four times higher in stroma lamellae vesicles than in inside-out vesicles. The proportion of the light-harvesting chlorophyll-a/b--protein complex in stroma lamellae vesicles increased from 13% to 21% of their total chlorophyll after phosphorylation of the thylakoids. There was also a corresponding increase in the level of chlorophyll b. These observations strongly suggest that phosphorylated light-harvesting complexes migrate from appressed thylakoids rich in photosystem 2 to non-appressed thylakoids rich in photosystem 1. In contrast, there was no evidence for a lateral migration of the chlorophyll-a--protein complex of photosystem 2 after phosphorylation. Our results indicate that a lateral migration of phosphorylated light-harvesting complexes in combination with a lateral separation of photosystem 1 and 2 to the different thylakoid regions, is a basis for the regulation of excitation energy between the two photosystems.
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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/Light-Harvesting Protein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Photosynthetic Reaction Center...,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
136
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
25-9
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:6352263-Chemical Phenomena,
pubmed-meshheading:6352263-Chemistry,
pubmed-meshheading:6352263-Chlorophyll,
pubmed-meshheading:6352263-Chloroplasts,
pubmed-meshheading:6352263-Light-Harvesting Protein Complexes,
pubmed-meshheading:6352263-Phosphates,
pubmed-meshheading:6352263-Photophosphorylation,
pubmed-meshheading:6352263-Photosynthesis,
pubmed-meshheading:6352263-Photosynthetic Reaction Center Complex Proteins,
pubmed-meshheading:6352263-Plant Proteins
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pubmed:year |
1983
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pubmed:articleTitle |
Changes in the lateral distribution of the light-harvesting chlorophyll-a/b--protein complex induced by its phosphorylation.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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