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1.
Prikl Biokhim Mikrobiol ; 49(3): 229-35, 2013.
Article in Russian | MEDLINE | ID: mdl-23882940

ABSTRACT

The review summarizes the results of studies on the comigration of tubercular bacteria and bean plants to new habitats, which is often accompanied by a decrease in the symbiosis efficiency due to a loss of the diversity of genes responsible for the interaction. This migration may lead to a rise in new symbionts as a result of gene transfers from initial symbionts to local bacteria. It was demonstrated that typically new symbionts lack an ability for N2 fixation but are highly competitive, blocking the inoculation of bean cultures by industrial strains. The design of coadapted systems of recognition and signal interaction of partners is a perspective approach to ensure competitive advantages of efficient rhizobia strains introduced into agrocenoses, together with host plants, over inactive local strains.


Subject(s)
Fabaceae/genetics , Rhizobium/genetics , Root Nodules, Plant/genetics , Symbiosis/genetics , Ecosystem , Nitrogen Fixation/genetics , Plant Physiological Phenomena , Plant Roots , Root Nodules, Plant/microbiology , Root Nodules, Plant/physiology , Species Specificity
2.
Mol Plant Microbe Interact ; 13(8): 799-807, 2000 Aug.
Article in English | MEDLINE | ID: mdl-10939251

ABSTRACT

Nod factors (NFs) are rhizobial lipo-chitooligosaccharide signals that trigger root nodule development in legumes. Modifications of NF structures influence their biological activity and affect their degradation by plant chitinases. Nodulation of certain pea cultivars by Rhizobium leguminosarum bv. viciae requires modification of NFs at the reducing end by either an O-acetyl or a fucosyl group. Fucosylated NFs were produced by an in vitro reaction with NodZ fucosyltransferase and purified. Their biological activity on pea was tested by measuring their capacity to stimulate the activity of a hydrolase that cleaves NFs. Nonmodified and fucosylated NFs displayed this activity at nano- to picomolar concentrations, while a sulfated NF from Sinorhizobium meliloti was inactive. In an additional series of experiments, the stability of non-modified and fucosylated NFs in the presence of purified tobacco chitinases was compared. The presence of the fucosyl group affected the degradation rates and the accessibility of specific cleavage sites on the chitooligosaccharide backbone. These results suggest that the fucosyl group in NFs also weakens the interaction of NFs with certain chitinases or chitinase-related proteins in pea roots.


Subject(s)
Chitinases/metabolism , Fucose/metabolism , Lipopolysaccharides/metabolism , Pisum sativum/metabolism , Rhizobium leguminosarum/metabolism , Chromatography, High Pressure Liquid , Kinetics , Lipopolysaccharides/isolation & purification , Plant Roots/metabolism , Plants, Toxic , Nicotiana/enzymology
3.
Mol Plant Microbe Interact ; 12(3): 252-8, 1999 Mar.
Article in English | MEDLINE | ID: mdl-10065561

ABSTRACT

We have analyzed the nucleotide sequences of the nodX genes from two strains of Rhizobium leguminosarum bv. viciae able to nodulate Afghan peas (strains A1 and Himalaya) and from two strains of R. leguminosarum bv. trifolii (ANU843 and CSF). The nodX genes of strains A1 and ANU843 were shown to be functional for the induction of nodules on Afghan peas. To analyze the cause of phenotypic differences of strain A1 and strain TOM we have studied the composition of the lipochitin-oligosaccharides (LCOs) produced by strain A1 after induction by the flavonoid naringenin or various pea root exudates. The structural analysis of the LCOs by mass spectrometry revealed that strain A1 synthesizes a family of at least 23 different LCOs. The use of exudates instead of naringenin resulted only in quantitative differences in the ratios of various LCOs produced.


Subject(s)
Bacterial Proteins/genetics , Genes, Bacterial , Rhizobium leguminosarum/genetics , Amino Acid Sequence , Bacterial Proteins/chemistry , Chromatography, High Pressure Liquid , Mass Spectrometry , Molecular Sequence Data , Sequence Homology, Amino Acid , Species Specificity
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