The genome of the versatile nitrogen fixer
BMC Genomics, 2008 Background Biological nitrogen fixation is a prokaryotic process that plays an essential role in the global nitrogen cycle. Azorhizobium caulinodans ORS571 has the dual capacity to fix nitrogen both as free-living organism and in a symbiotic interaction ...
Binnewies Tim T +20 more
doaj +8 more sources
Stringent Expression Control of Pathogenic R-body Production in Legume Symbiont
mBio, 2017 R bodies are insoluble large polymers consisting of small proteins encoded by reb genes and are coiled into cylindrical structures in bacterial cells.
Jun-ichi Matsuoka +8 more
doaj +5 more sources
Oxalic Acid From Sesbania rostrata Seed Exudates Mediates the Chemotactic Response of Azorhizobium caulinodans ORS571 Using Multiple Strategies [PDF]
Frontiers in Microbiology, 2019 Chemotaxis toward seed exudates is important in the establishment of microbe–plant associations. The objective of this work was to explore whether organic acids from the seed exudates of Sesbania rostrata play a role in recruiting Azorhizobium ...
Xiaolin Liu +8 more
doaj +2 more sources
Azorhizobium caulinodans Transmembrane Chemoreceptor TlpA1 Involved in Host Colonization and Nodulation on Roots and Stems [PDF]
Frontiers in Microbiology, 2017 Azorhizobium caulinodans ORS571 is a motile soil bacterium that interacts symbiotically with legume host Sesbania rostrata, forming nitrogen-fixing root and stem nodules.
Wei Liu +9 more
doaj +2 more sources
Identification of Cbp1, a c-di-GMP Binding Chemoreceptor in Azorhizobium caulinodans ORS571 Involved in Chemotaxis and Nodulation of the Host Plant [PDF]
Frontiers in Microbiology, 2019 Cbp1, a chemoreceptor containing a PilZ domain was identified in Azorhizobium caulinodans ORS571, a nitrogen-fixing free-living soil bacterium that induces nodule formation in both the roots and stems of the host legume Sesbania rostrata.
Yu Sun +8 more
doaj +2 more sources
Rhizopine biosensors for plant-dependent control of bacterial gene expression. [PDF]
Environ Microbiol, 2023 Abstract Engineering signalling between plants and microbes could be exploited to establish host‐specificity between plant‐growth‐promoting bacteria and target crops in the environment. We previously engineered rhizopine‐signalling circuitry facilitating exclusive signalling between rhizopine‐producing (RhiP) plants and model bacterial strains.
Haskett TL +11 more
europepmc +2 more sources
Azorhizobium caulinodans ORS571 Colonizes the Xylem of Arabidopsis thaliana [PDF]
Molecular Plant-Microbe Interactions, 2001 Improved conditions were used for the aseptic growth of Arabidopsis thaliana to investigate whether xylem colonization of A. thaliana by Azorhizobium caulinodans ORS571 might occur. When seedlings were inoculated with ORS571 (pXLGD4) tagged with the lacZ
Philip J. Stone +3 more
doaj +3 more sources
Overexpression of the Chromosome Partitioning Gene parA in Azorhizobium caulinodans ORS571 Alters the Bacteroid Morphotype in Sesbania rostrata Stem Nodules [PDF]
Frontiers in Microbiology, 2019 Azorhizobium caulinodans ORS571 is a diazotroph that forms N2-fixing nodules on the roots and stems of the tropical legume Sesbania rostrata. Deletion of the parA gene of this bacterium results in cell cycle defects, pleiomorphic cell shape, and ...
Hsiao-Lin Chien +5 more
doaj +2 more sources
Metabolic Engineering of the 5-Aminolevulinate Biosynthetic Pathway in E. coli Improves Efficiency of Hemoprotein-Based Biocatalysis. [PDF]
Angew Chem Int Ed EnglWe have engineered the heme biosynthetic pathway in E. coli to develop an efficient cofactor supplementation system for hemoproteins. Through the incorporation of the heterogeneous C4 pathway, the engineered cells significantly increase the expression levels of active holohemoproteins and enhance the efficiency of whole‐cell and lysate‐based ...
Kato S +6 more
europepmc +3 more sources
Cyanuric acid hydrolase from Azorhizobium caulinodans ORS 571: crystal structure and insights into a new class of Ser-Lys dyad proteins. [PDF]
PLoS ONE, 2014 Cyanuric acid hydrolase (CAH) catalyzes the hydrolytic ring-opening of cyanuric acid (2,4,6-trihydroxy-1,3,5-triazine), an intermediate in s-triazine bacterial degradation and a by-product from disinfection with trichloroisocyanuric acid.
Seunghee Cho +5 more
doaj +2 more sources