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Symbiotic host-specificity of Rhizobium meliloti is determined by a sulphated and acylated glucosamine oligosaccharide signal

Nature volume 344, pages 781–784 (1990)Cite this article

Abstract

RHIZOBIA are symbiotic bacteria that elicit the formation on leguminous plants of specialized organs, root nodules, in which they fix nitrogen1. In various Rhizobium species, such as R. leguminosarum and R. meliloti, common and host-specific nodullation (nod) genes have been identified which determine infection and nodulation of specific hosts1. Common nod ABC genes2–5 as well as host-specific nodH and nodQ genes4'6–8 were shown recently, using bioassays, to be involved in the production of extracellular Nod signals. Using R. meliloti strains overproducing symbiotic Nod factors, we have purified the major alfalfa-specific signal, NodRm-1, by gel permeation, ion exchange and C18 reverse-phase high performance liquid chromatography. From mass spec-trometry, nuclear magnetic resonance, 35S-labelling and chemical modification studies, NodRm-1 was shown to be a sulphated β-1,4-tetrasaccharide of D-glucosamine (Mr 1,102) in which three amino groups were acetylated and one was acylated with a C16 bis-unsaturated fatty acid. This purified Nod signal specifically elicited root hair deformation on the homologous host when added in nanomolar concentration.

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Affiliations

  1. Centre de Recherches de Biochimie et de Génétique Cellulaire, CNRS LP8201, 118 Route de Narbonne, 31062, Toulouse Cedex, France

    Patrice Lerouge, Philippe Roche & Jean Claude Promé

  2. Laboratoire de Biologie Moléculaire des Relations Plantes-Microorganismes, CNRS-INRA, BP27, 31326, Castanet-Tolosan Cedex, France

    Catherine Faucher, Fabienne Maillet, Georges Truchet & Jean Dénarié

Authors
  1. Patrice Lerouge
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  2. Philippe Roche
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  3. Catherine Faucher
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  4. Fabienne Maillet
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  5. Georges Truchet
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  6. Jean Claude Promé
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  7. Jean Dénarié
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Lerouge, P., Roche, P., Faucher, C. et al. Symbiotic host-specificity of Rhizobium meliloti is determined by a sulphated and acylated glucosamine oligosaccharide signal. Nature 344, 781–784 (1990). https://doi.org/10.1038/344781a0

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