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PMID: 2330031 Published · ppublish English Journal Article

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

Nature ·Vol. 344 ·No. 6268 ·1990-04-19 ·Pages 781-4

Lerouge P, Roche P, Faucher C, Maillet F, Truchet G, Promé JC, Dénarié J

Abstract

Rhizobia are symbiotic bacteria that elicit the formation on leguminous plants of specialized organs, root nodules, in which they fix nitrogen. In various Rhizobium species, such as R. leguminosarum and R. meliloti, common and host-specific nodulation (nod) genes have been identified which determine infection and nodulation of specific hosts. Common nodABC genes as well as host-specific nodH and nodQ genes 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 spectrometry, nuclear magnetic resonance, (35)S-labelling and chemical modification studies, NodRm-1 was shown to be a sulphated beta-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.

MeSH Terms
Acylation Acyltransferases Bacterial Outer Membrane Proteins/genetics Bacterial Proteins/genetics Carbohydrate Sequence Genes, Bacterial Magnetic Resonance Spectroscopy Mass Spectrometry Medicago sativa/microbiology Molecular Sequence Data Molecular Structure Mutation N-Acetylglucosaminyltransferases Oligosaccharides/genetics,metabolism Plasmids Rhizobium/genetics,metabolism Signal Transduction Sulfates/metabolism Symbiosis Transfection
Chemicals
Bacterial Outer Membrane Proteins Bacterial Proteins NodD protein, Bacteria Oligosaccharides Sulfates NodRM-1 Acyltransferases NodA protein, Rhizobiales N-Acetylglucosaminyltransferases NodC protein, Rhizobiales
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Lerouge P
Centre de Recherches de Biochimie et de Génétique Cellulaire, CNRS LP8201, Toulouse, France.
Roche P
Faucher C
Maillet F
Truchet G
Promé J C
Dénarié J
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1990-04-19
Pages
781-4
Language
English
Region
England
NLM ID
0410462
Subset
IM
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