High impact information on FT1

• Xyloglucan fucosyltransferase, an enzyme involved in plant cell wall biosynthesis [1].
• Antibodies raised against recombinant AtFTase immunoprecipitate FTase enzyme activity from solubilized Arabidopsis membrane proteins, and AtFT1 expressed in mammalian COS cells results in the presence of XG FTase activity in these cells [1].
• Because the mur1 mutation affects several cell wall polysaccharides, whereas the mur2 mutation is specific to xyloglucan, the phenotypes of mur1 plants appear to be caused by structural changes in fucosylated pectic components such as rhamnogalacturonan-II [2].
• O-Acetylation of galactose residues was considerably reduced in Fuc-deficient mutants (atfut1, mur1, and mur2) that synthesize XyG containing little or no Fuc [3].
• From comparison of the mechanical responses of mur2 and mur3, we deduce that galactose-containing side chains of xyloglucan make a major contribution to overall wall strength, whereas xyloglucan fucosylation plays a comparatively minor role [4].

Associations of FT1 with chemical compounds

• No Fuc was detected in XyG derived from leaves or roots of atfut1 [3].
• Mutants with reductions in a single monosaccharide have been identified for fucose (mur2, mur3), arabinose (mur4, mur5, mur6, mur7), and rhamnose (mur8) [5].

References