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Literature summary for 2.1.1.68 extracted from

  • Tu, Y.; Rochfort, S.; Liu, Z.; Ran, Y.; Griffith, M.; Badenhorst, P.; Louie, G.V.; Bowman, M.E.; Smith, K.F.; Noel, J.P.; Mouradov, A.; Spangenberg, G.
    Functional analyses of caffeic acid O-methyltransferase and cinnamoyl-CoA-reductase genes from perennial ryegrass (Lolium perenne) (2010), Plant Cell, 22, 3357-3373.
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Lolium perenne
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-
-

Source Tissue

Source Tissue Comment Organism Textmining
internode
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 Lolium perenne
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stem
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 Lolium perenne
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Synonyms

Synonyms Comment Organism
O-methyltransferase
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 Lolium perenne
OMT1
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 Lolium perenne
OMT3
-
 Lolium perenne

Expression

Organism Comment Expression
Lolium perenne expression of both OMT1 and OMT3 genes is elevated during the early elongation (E1) stage. OMT1 shows low expression at E2 and E3 stages and is strongly upregulated at the R1 stage, with the highest level of expression in the uppermost internode. Both OMT3 and OMT1 genes show a low level of expression at R2 and R3 developmental stages additional information
Lolium perenne expression of both OMT1 and OMT3 genes is elevated during the early elongation (E1) stage. OMT3 shows almost complementary expression profiles to OMT1 at the E2, E3, and R1 stages with low expression at R1 stage. Both OMT3 and OMT1 genes show a low level of expression at R2 and R3 developmental stages additional information

General Information

General Information Comment Organism
malfunction downregulation of CCR1 and caffeic acid O-methyltransferase 1 (OMT1) using an RNA interference-mediated silencing strategy causes dramatic changes in lignin level and composition in transgenic perennial ryegrass plants grown under both glasshouse and field conditions. Both field-grown OMT1-deficient and CCR1-deficient perennial ryegrass plants show enhanced digestibility without obvious detrimental effects on either plant fitness or biomass production Lolium perenne
physiological function OMT1 plays a key role in biosynthesis of both syringyl- and guaiacyl-lignin subunits in perennial ryegrass Lolium perenne