title: NodZ of Bradyrhizobium extends the nodulation host range of Rhizobium by adding a fucosyl residue to nodulation signals.
abstract: The nodulation genes of rhizobia are involved in the production of the lipo-chitin oligosaccharides (LCO), which are signal molecules required for nodule formation. A mutation in nodZ of Bradyrhizobium japonicum results in the synthesis of nodulation signals lacking the wild-type 2-O-methylfucose residue at the reducting-terminal N-acetylglucosamine. This phenotype is correlated with a defective nodulation of siratro (Macroptilium atropurpureum). Here we show that transfer of nodZ to Rhizobium leguminosarum blovar (bv) viciae, which produces LCOs that are not modified at the reducing-terminal N-acetylglucosamine, results in production of LCOs with a fucosyl residue on C-6 of the reducing-terminal N-acetylglucosamine. This finding, together with in vitro enzymatic assays, indicates that the product of nodZ functions as a fucosyltransferase. The transconjugant R. leguminosarum strain producing fucosylated LCOs acquires the capacity to nodulate M. atropurpureum, Glycine soja, Vigna unguiculate and Leucaena leucocephala. Therefore, nodZ extends the narrow host range of R. leguminosarum bv. viciae to include various tropical legumes. However, microscopic analysis of nodules induced on siratro shows that these nodules do not contain bacteroids, showing that transfer of nodZ does not allow R. leguminosarum to engage in a nitrogen-fixing symbiosis with this plant.
authors.affiliation: Institute of Molecular Plant Sciences, Leiden University, The Netherlands.
authors.forename: I M
authors.initials: IM
authors.lastname: López-Lara
authors.forename: L
authors.initials: L
authors.lastname: Blok-Tip
authors.forename: C
authors.initials: C
authors.lastname: Quinto
authors.forename: M L
authors.initials: ML
authors.lastname: Garcia
authors.forename: G
authors.initials: G
authors.lastname: Stacey
authors.forename: G V
authors.initials: GV
authors.lastname: Bloemberg
authors.forename: G E
authors.initials: GE
authors.lastname: Lamers
authors.forename: B J
authors.initials: BJ
authors.lastname: Lugtenberg
authors.forename: J E
authors.initials: JE
authors.lastname: Thomas-Oates
authors.forename: H P
authors.initials: HP
authors.lastname: Spaink
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D002240:Carbohydrate Sequence; D003001:Cloning, Molecular; D003227:Conjugation, Genetic; D007887:Fabaceae / Q000382:microbiology; D005643:Fucose / Q000737:chemistry; D005647:Fucosyltransferases / Q000235:genetics* / Q000378:metabolism*; D005798:Genes, Bacterial; D008070:Lipopolysaccharides / Q000096:biosynthesis / Q000737:chemistry; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009154:Mutation; D009586:Nitrogen Fixation / Q000235:genetics* / Q000502:physiology; D010641:Phenotype; D010946:Plants, Medicinal; D011401:Promoter Regions, Genetic; D012230:Rhizobiaceae / Q000235:genetics* / Q000378:metabolism; D016961:Rhizobium leguminosarum / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction; D013559:Symbiosis
chemical_list: D001426:Bacterial Proteins; D008070:Lipopolysaccharides; C023023:lipid-linked oligosaccharides; D005643:Fucose; D005647:Fucosyltransferases; C103941:NodZ protein, bacteria