Carbohydrate binding activities of Bradyrhizobium japonicum. I. Saccharide-specific inhibition of homotypic and heterotypic adhesion.
TLDR
All four of the saccharide-inhibitable binding activities of Bradyrhizobium japonicum may be mediated by the same mechanism(s) or molecular component(s).Abstract:
Bradyrhizobium japonicum (R110d) exhibited four saccharide-specific binding activities: (a) adsorption to Sepharose beads containing covalently coupled lactose; (b) homotypic agglutination through one pole of the cell (star formation); (c) heterotypic adhesion to the cultured soybean cell line, SB-1; and (d) attachment to roots of soybean plants. Each of these binding activities can be inhibited by the addition of galactose or lactose, but not by derivatives such as N-acetyl-D-galactosamine or melibiose. Treatment of wild-type bacteria with N-methyl-N'-nitro-N-nitrosoguanidine followed by selection on the basis of reduced binding to SB-1 cells, resulted in two specific mutants, designated N4 and N6. Compared to wild type, these two mutants also exhibited decreased binding activity in: (a) adsorption to lactose-Sepharose beads; (b) homotypic star formation; and (c) heterotypic attachment to roots of soybeans plants. These results suggest that all four of the saccharide-inhibitable binding activities of Bradyrhizobium japonicum may be mediated by the same mechanism(s) or molecular component(s).read more
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The Rhizobium-plant symbiosis.
P van Rhijn,Jozef Vanderleyden +1 more
TL;DR: An overview of the organization, regulation, and function of the nod genes and their participation in the determination of the host specificity is presented.
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Molecular mechanisms of attachment of Rhizobium bacteria to plant roots.
TL;DR: This review covers the current knowledge on one of the best‐studied examples of bacterium‐plant attachment, namely the molecular mechanism by which Rhizobium bacteria adhere to plant roots.
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Rhizobial secreted proteins as determinants of host specificity in the rhizobium-legume symbiosis.
Maarten Fauvart,Jan Michiels +1 more
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A unipolarly located, cell-surface-associated agglutinin, RapA, belongs to a family of Rhizobium-adhering proteins (Rap) in Rhizobium leguminosarum bv. trifolii.
TL;DR: It is proposed that the homologous Ra domains, found to be present also in other proteins with different structure, represent lectin domains, which confer upon these proteins the ability to recognize their cognate carbohydrate structures.
References
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
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Nathan Sharon,Halina Lis +1 more
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TL;DR: The evidence suggests that an interaction between legume lectins and Rhizobium cells may account for the specificity expressed between rhizobia and host plant in the initiation of the nitrogen-fixing symbiosis.
Journal ArticleDOI
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