Disease relevance of nodB

• E. coli strains, harboring nodA and/or nodB, did not produce Nod metabolites, whereas the strain expressing nodC produced chitooligosaccharides [1].
• Protein sequence comparisons revealed significant similarities of the fungal chitin deacetylase to rhizobial nodB proteins and to an uncharacterized protein encoded by a Bacillus stearothermophilus open reading frame [2].
• Unlike the case with other Rhizobium strains examined to date, nodB was found on an operon separate from nodACIJ [3].
• In 1992 a second group reported a failure to find any evidence of functional complementation of various rhizobial nod mutants by Frankia DNA (nodA, nodB and nodC) [4].
• Novel cellulose-binding domains, NodB homologues and conserved modular architecture in xylanases from the aerobic soil bacteria Pseudomonas fluorescens subsp. cellulosa and Cellvibrio mixtus [5].

High impact information on nodB

• These results confirm previous reports that NodB is an N-deacetylase and suggest that NodA is an N-acyltransferase [6].
• The monosaccharide N-acetylglucosamine is not deacetylated by NodB [7].
• XYLE contained a glycosyl hydrolase family 11 catalytic domain at its N-terminus, followed by three other domains; the second of these exhibited sequence identity with NodB from rhizobia [5].
• We analysed 54 strains from several populations distributed in the Northern Hemisphere, using nucleotide sequences of three 'core' chromosomal genes (rrs, glnII and atpD) and two 'auxiliary' symbiotic genes (nifH and nodB) to elucidate the biogeographic history of the species and symbiotic ecotypes (biovarieties) within species [8].

Chemical compound and disease context of nodB

• Our data show that the NodB protein of Rhizobium meliloti deacetylates the nonreducing N-acetylglucosamine residue of chitooligosaccharides [7].

Biological context of nodB

• The 9.2-kb fragment complemented nodA-, nodB-, and nodC- mutants of R. meliloti to the Nod+ phenotype on Medicago sativa, M. truncatula, and Trigonella foenum-graecum [9].

Associations of nodB with chemical compounds

• Analysis of GlcNAc metabolites from various mutants, e.g., nodA-, nodB-, or nodC- mutants, should facilitate the identification of the in vivo substrates involved in the synthesis of the "common" Nod factor and, thereby, lead to a greater understanding of Nod factor biosynthesis and transport [10].
• The basic structure of the Nod signal, an acylated oligomer of N-acetylglucosamine, is synthesized through the action of NodA, NodB, and NodC [11].

Analytical, diagnostic and therapeutic context of nodB

• Sequence analysis of the nodACIJ and nodB operon regions confirm that R. loti common nod genes have a gene organization different from that of other Rhizobium spp [3].

References