A. Day et al., Caffeoyl-coenzyme A 3-O-methyltransferase enzyme activity, protein and transcript accumulation in flax (Linum usitatissimum) stem during development, PHYSL PLANT, 113(2), 2001, pp. 275-284
Flax (Linum usitatissimum) is a commercially important fiber crop in Europe
. Lignification of its phloem fibers, although weak, causes a decrease in t
heir commercial quality. In flax, fiber lignin mainly consists of guaiacyl
(G) units in contrast to the mixed guaiacyl-syringyl (G-S) lignin type occu
rring in xylem fibers. G lignins are reported as more condensed polymers du
e to a higher frequency of 5-5 linkages, whereas the deposition of syringyl
end groups in lignins increases the proportion of alky-aryl ether linkages
as beta -O-4-bonds. The type of linkages within a lignin polymer depends o
n the methylation of either the 3-hydroxyl groups or both 3-OH and 5-OH gro
ups, which is controlled by two enzymes: caffeate 3-O-methyttransferase (CO
MT) and caffeoyl-coenzyme A 3-O-methyltransferase (CCoAOMT). First, we meas
ured the in vitro activity of both OMTs in the flax stem tissues during ste
m development. CCoAOMT activity varied in the same way as COMT, i.e. increa
sed gradually with stem maturity, from the top to the bottom of the stem, w
as maximum at the flowering stage and was lower, but still scorable, in the
outer fiber-bearing tissues than in the xylem cells. In a second step, we
focused our studies on the characterization of CCoAOMT in order to understa
nd the implication of this enzyme in the lignification of flax fiber cells.
CCoAOMT activity appeared to be associated with the accumulation of an aci
dic 33-kDa polypeptide identified as a CCoAOMT after immunological cross-re
activity with a poplar CCoAOMT and microsequencing. The differential accumu
lation of the CCoAOMT protein was confirmed by immunolocalization on tissue
prints and correlated with that of the transcripts, suggesting a transcrip
tional regulation of CCoAOMT in the flax stem.