NMR characterization of lignins in Arabidopsis altered in the activity of ferulate 5-hydroxylase

Proc Natl Acad Sci U S A. 1999 Oct 26;96(22):12328-32. doi: 10.1073/pnas.96.22.12328.

Abstract

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.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Arabidopsis / chemistry*
  • Arabidopsis / enzymology
  • Arabidopsis Proteins*
  • Cytochrome P-450 Enzyme System*
  • Lignin / chemistry*
  • Magnetic Resonance Spectroscopy
  • Mixed Function Oxygenases / metabolism*
  • Plant Proteins / metabolism*
  • Plants, Genetically Modified / chemistry
  • Plants, Genetically Modified / enzymology

Substances

  • Arabidopsis Proteins
  • Plant Proteins
  • Lignin
  • Cytochrome P-450 Enzyme System
  • Mixed Function Oxygenases
  • CYP84A1 protein, Arabidopsis