pubmed-article:1592815 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1592815 | lifeskim:mentions | umls-concept:C0085356 | lld:lifeskim |
pubmed-article:1592815 | lifeskim:mentions | umls-concept:C0002728 | lld:lifeskim |
pubmed-article:1592815 | lifeskim:mentions | umls-concept:C0002732 | lld:lifeskim |
pubmed-article:1592815 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
pubmed-article:1592815 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
pubmed-article:1592815 | lifeskim:mentions | umls-concept:C2247328 | lld:lifeskim |
pubmed-article:1592815 | lifeskim:mentions | umls-concept:C0205349 | lld:lifeskim |
pubmed-article:1592815 | pubmed:issue | 11 | lld:pubmed |
pubmed-article:1592815 | pubmed:dateCreated | 1992-7-1 | lld:pubmed |
pubmed-article:1592815 | pubmed:abstractText | Amylose-defective mutants were selected after UV mutagenesis of Chlamydomonas reinhardtii cells. Two recessive nuclear alleles of the ST-2 gene led to the disappearance not only of amylose but also of a fraction of the amylopectin. Granule-bound starch synthase activities were markedly reduced in strains carrying either st-2-1 or st-2-2, as is the case for amylose-deficient (waxy) endosperm mutants of higher plants. The main 76-kDa protein associated with the starch granule was either missing or greatly diminished in both mutants, while st-2-1-carrying strains displayed a novel 56-kDa major protein. Methylation and nuclear magnetic resonance analysis of wild-type algal storage polysaccharide revealed a structure identical to that of higher-plant starch, while amylose-defective mutants retained a modified amylopectin fraction. We thus propose that the waxy gene product conditions not only the synthesis of amylose from endosperm storage tissue in higher-plant amyloplasts but also that of amylose and a fraction of amylopectin in all starch-accumulating plastids. The nature of the ST-2 (waxy) gene product with respect to the granule-bound starch synthase activities is discussed. | lld:pubmed |
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pubmed-article:1592815 | pubmed:language | eng | lld:pubmed |
pubmed-article:1592815 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1592815 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:1592815 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1592815 | pubmed:month | Jun | lld:pubmed |
pubmed-article:1592815 | pubmed:issn | 0021-9193 | lld:pubmed |
pubmed-article:1592815 | pubmed:author | pubmed-author:BalkRR | lld:pubmed |
pubmed-article:1592815 | pubmed:author | pubmed-author:FournetBB | lld:pubmed |
pubmed-article:1592815 | pubmed:author | pubmed-author:DecqAA | lld:pubmed |
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pubmed-article:1592815 | pubmed:author | pubmed-author:FontaineTT | lld:pubmed |
pubmed-article:1592815 | pubmed:author | pubmed-author:DelrueBB | lld:pubmed |
pubmed-article:1592815 | pubmed:author | pubmed-author:RoutierFF | lld:pubmed |
pubmed-article:1592815 | pubmed:author | pubmed-author:Van Den... | lld:pubmed |
pubmed-article:1592815 | pubmed:author | pubmed-author:MaddeleinM... | lld:pubmed |
pubmed-article:1592815 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1592815 | pubmed:volume | 174 | lld:pubmed |
pubmed-article:1592815 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1592815 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1592815 | pubmed:pagination | 3612-20 | lld:pubmed |
pubmed-article:1592815 | pubmed:dateRevised | 2010-9-9 | lld:pubmed |
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pubmed-article:1592815 | pubmed:year | 1992 | lld:pubmed |
pubmed-article:1592815 | pubmed:articleTitle | Waxy Chlamydomonas reinhardtii: monocellular algal mutants defective in amylose biosynthesis and granule-bound starch synthase activity accumulate a structurally modified amylopectin. | lld:pubmed |
pubmed-article:1592815 | pubmed:affiliation | Laboratoire de Chimie Biologique, Université des Sciences et Techniques de Lille Flandres-Artois 59655, Villeneuve d'Ascq, France. | lld:pubmed |
pubmed-article:1592815 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1592815 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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