Source:http://linkedlifedata.com/resource/pubmed/id/10535921
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
22
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pubmed:dateCreated |
1999-12-10
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pubmed:abstractText |
Nuclear magnetic resonance (NMR) of isolated lignins from an Arabidopsis mutant deficient in ferulate 5-hydroxylase (F5H) and transgenic plants derived from the mutant by overexpressing the F5H gene has provided detailed insight into the compositional and structural differences between these lignins. Wild-type Arabidopsis has a guaiacyl-rich, syringyl-guaiacyl lignin typical of other dicots, with prominent beta-aryl ether (beta-O-4), phenylcoumaran (beta-5), resinol (beta-beta), biphenyl/dibenzodioxocin (5-5), and cinnamyl alcohol end-group structures. The lignin isolated from the F5H-deficient fah1-2 mutant contained only traces of syringyl units and consequently enhanced phenylcoumaran and dibenzodioxocin levels. In fah1-2 transgenics in which the F5H gene was overexpressed under the control of the cauliflower mosaic virus 35S promoter, a guaiacyl-rich, syringyl/guaiacyl lignin similar to the wild type was produced. In contrast, the isolated lignin from the fah1-2 transgenics in which F5H expression was driven by the cinnamate 4-hydroxylase promoter was almost entirely syringyl in nature. This simple lignin contained predominantly beta-aryl ether units, mainly with erythro-stereochemistry, with some resinol structures. No phenylcoumaran or dibenzodioxocin structures (which require guaiacyl units) were detectable. The overexpression of syringyl units in this transgenic resulted in a lignin with a higher syringyl content than that in any other plant we have seen reported.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535921-10430877,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535921-10468559,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535921-1477555,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535921-8692910,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535921-9211851,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535921-9618461,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10535921-9788995
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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/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/CYP84A1 protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 Enzyme System,
http://linkedlifedata.com/resource/pubmed/chemical/Lignin,
http://linkedlifedata.com/resource/pubmed/chemical/Mixed Function Oxygenases,
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 |
0027-8424
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
96
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12328-32
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pubmed:dateRevised |
2010-9-13
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pubmed:meshHeading |
pubmed-meshheading:10535921-Arabidopsis,
pubmed-meshheading:10535921-Arabidopsis Proteins,
pubmed-meshheading:10535921-Cytochrome P-450 Enzyme System,
pubmed-meshheading:10535921-Lignin,
pubmed-meshheading:10535921-Magnetic Resonance Spectroscopy,
pubmed-meshheading:10535921-Mixed Function Oxygenases,
pubmed-meshheading:10535921-Plant Proteins,
pubmed-meshheading:10535921-Plants, Genetically Modified
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pubmed:year |
1999
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pubmed:articleTitle |
NMR characterization of lignins in Arabidopsis altered in the activity of ferulate 5-hydroxylase.
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pubmed:affiliation |
United States Dairy Forage Research Center, United States Department of Agriculture, Agricultural Research Service, Madison, WI 53706-1108, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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