Fucosylated arabinogalactan-proteins are required for full root cell elongation in arabidopsis.
The Arabidopsis thaliana mutant mur1 is affected in the biosynthesis of l-fucose and has less than 2% of the normal amounts of this sugar in the cell walls of its aerial parts. Although in roots the reduction of l-fucose is only 40%, this causes a decrease of about 50% in root cell elongation. Since arabinogalactan-proteins (AGPs) are known to play a role in plant cell expansion we studied the composition of mur1 root AGPs. Arabidopsis root AGPs were shown to contain l-fucose, which was reduced in level in mur1 AGPs. In wild-type plants, an l-fucose containing epitope is present in AGPs in the cell wall of differentiating root cells. Addition of eel lectin, which specifically recognizes this epitope, and not fucose in other wall polymers, can phenocopy mur1 roots. Several lines of evidence are presented to support the contention that l-fucose containing root AGPs are required for the full elongation of root cells.
D000818:Animals; D017360:Arabidopsis / Q000235:genetics / Q000254:growth & development* / Q000378:metabolism; D002455:Cell Division / Q000235:genetics / Q000502:physiology; D002473:Cell Wall / Q000378:metabolism; D004524:Eels; D000939:Epitopes / Q000235:genetics / Q000378:metabolism; D005643:Fucose / Q000378:metabolism*; D005647:Fucosyltransferases / Q000378:metabolism; D005960:Glucosides; D006154:Guanosine Diphosphate Fucose / Q000378:metabolism; D037102:Lectins / Q000494:pharmacology; D018613:Microscopy, Confocal; D009088:Mucoproteins / Q000378:metabolism*; D009154:Mutation; D010641:Phenotype; D010696:Phloroglucinol / Q000031:analogs & derivatives*; D010940:Plant Proteins; D018517:Plant Roots / Q000166:cytology / Q000254:growth & development* / Q000378:metabolism
D000939:Epitopes; D005960:Glucosides; D037102:Lectins; D009088:Mucoproteins; D010940:Plant Proteins; C104977:Yariv reagent; C006619:arabinogalactan proteins; D006154:Guanosine Diphosphate Fucose; D005643:Fucose; D010696:Phloroglucinol; D005647:Fucosyltransferases