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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1989-1-3
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pubmed:abstractText |
The photosystem I complex of the green alga Chlamydomonas reinhardtii was isolated and fractionated into its two subcomplex components: the core complex (CC I), which contained the reaction center (P-700) and had four polypeptide subunits, and the light-harvesting complex (LHC I) which contained four polypeptides of about 22, 25, 26 and 27 kDa. The 22-kDa apoprotein was isolated as a chlorophyll a and b binding protein. In the isolated photosystem I holocomplex, about ten copies of the 22-kDa LHC I apoprotein are present for each CC I unit. The 22-kDa polypeptide as well as the other three polypeptides of this complex and the subunit II of CC I are translated on 80S cytoplasmic ribosomes, and therefore are coded in the nucleus. During the greening process of the Chlamydomonas reinhardtii y-1 mutant the 22-kDa LHC I polypeptide, which cross-reacts with polyclonal antibodies raised against the Lemna gibba 20-kDa LHC I apoprotein, accumulates in thylakoids at a late stage of their development, and about 2-3 h after the LHC II and CC I subunit II polypeptides have accumulated. Accumulation of the 22-kDa protein during greening is inhibited by cycloheximide but not by chloramphenicol.
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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/Chloramphenicol,
http://linkedlifedata.com/resource/pubmed/chemical/Chlorophyll,
http://linkedlifedata.com/resource/pubmed/chemical/Cycloheximide,
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/Photosystem I Protein Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
177
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
411-6
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:3056724-Chlamydomonas,
pubmed-meshheading:3056724-Chloramphenicol,
pubmed-meshheading:3056724-Chlorophyll,
pubmed-meshheading:3056724-Chloroplasts,
pubmed-meshheading:3056724-Cycloheximide,
pubmed-meshheading:3056724-Cytoplasm,
pubmed-meshheading:3056724-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:3056724-Light-Harvesting Protein Complexes,
pubmed-meshheading:3056724-Photosynthesis,
pubmed-meshheading:3056724-Photosynthetic Reaction Center Complex Proteins,
pubmed-meshheading:3056724-Photosystem I Protein Complex,
pubmed-meshheading:3056724-Plant Proteins,
pubmed-meshheading:3056724-Protein Biosynthesis,
pubmed-meshheading:3056724-Ribosomes,
pubmed-meshheading:3056724-Spectrophotometry
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pubmed:year |
1988
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pubmed:articleTitle |
Structure and biogenesis of Chlamydomonas reinhardtii photosystem I.
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pubmed:affiliation |
Department of Biological Chemistry, Hebrew University of Jerusalem, Israel.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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