scholarly journals Isolation and characterization of a conjugative plasmid in a halo blight strain of Pseudomonas syringae pv. mori.

1984 ◽  
Vol 50 (1) ◽  
pp. 39-45
Author(s):  
Mamoru SATO
Keyword(s):  
Pseudomonas Syringae ◽  
Conjugative Plasmid ◽  
Halo Blight ◽  
Isolation And Characterization

scholarly journals Isolation and Characterization of the Gene Coding for the Amidinotransferase Involved in the Biosynthesis of Phaseolotoxin in Pseudomonas syringae pv. phaseolicola

2001 ◽  
Vol 14 (4) ◽  
pp. 545-554 ◽  
Author(s):  
Gustavo Hernández-Guzmán ◽  
Ariel Alvarez-Morales
Keyword(s):  
Aspartic Acid ◽  
Pseudomonas Syringae ◽  
Sequence Similarity ◽  
Insertion Mutant ◽  
Halo Blight ◽  
Streptomyces Spp ◽  
Isolation And Characterization ◽  
Gene Coding ◽  
Blight Disease

Pseudomonas syringae pv. phaseolicola is the causal agent of the “halo blight” disease of beans. A key component in the development of the disease is a nonhost-specific toxin, Nδ-(N'-sulphodiaminophosphinyl)-ornithyl-alanyl-homoarginine, known as phaseolotoxin. The homoarginine residue in this molecule has been suggested to be the product of Larginine:lysine amidinotransferase activity, previously detected in extracts of P. syringae pv. phaseolicola grown under conditions of phaseolotoxin production. We report the isolation and characterization of an amidinotransferase gene (amtA) from P. syringae pv. phaseolicola coding for a polypeptide of 362 residues (41.36 kDa) and showing approximately 40% sequence similarity to Larginine:inosamine-phosphate amidinotransferase from three species of Streptomyces spp. and 50.4% with an Larginine:glycine amidinotransferase from human mitochondria. The cysteine, histidine, and aspartic acid residues involved in substrate binding are conserved. Furthermore, expression of the amtA and argK genes and phaseolotoxin production occurs at 18°C but not at 28°C. An amidinotransferase insertion mutant was obtained that lost the capacity to synthesize homoarginine and phaseolotoxin. These results show that the amtA gene isolated is responsible for the amidinotransferase activity detected previously and that phaseolotoxin production depends upon the activity of this gene.

Isolation and Characterization of Bacteriophages Against Pseudomonas syringae pv. actinidiae Causing Bacterial Canker Disease in Kiwifruit

2016 ◽  
Vol 26 (2) ◽  
pp. 385-393 ◽  
Author(s):  
Ji-Gang Yu ◽  
Jeong-A Lim ◽  
Yu-Rim Song ◽  
Sunggi Heu ◽  
Gyoung Hee Kim ◽  
...  
Keyword(s):  
Pseudomonas Syringae ◽  
Bacterial Canker ◽  
Canker Disease ◽  
Isolation And Characterization

Isolation and characterization of syringacin W-1, a bacteriocin produced by Pseudomonas syringae pv. syringae

1986 ◽  
Vol 32 (3) ◽  
pp. 231-236 ◽  
Author(s):  
Mary L. Smidt ◽  
Anne K. Vidaver
Keyword(s):  
Pseudomonas Syringae ◽  
Inner Core ◽  
Deae Cellulose ◽  
Sedimentation Coefficient ◽  
Temperature Stability ◽  
Ultrafiltration Rate ◽  
Isolation And Characterization ◽  
Outer Sheath ◽  
Shaped Particle

Syringacin W-1, a bacteriocin produced by Pseudomonas syringae pathovar syringae strain PsW-1, is a 20 × 75 nm rod-shaped particle composed of an inner core and outer sheath. Production of syringacin W-1 in broth was induced with 0.1 μLg/mL mitomycin C. The bacteriocin was purified from culture lysates using ultrafiltration, rate zonal centrifugation in sucrose gradients, and DEAE-cellulose chromatography. Purity was evaluated by subjecting syringacin W-1 preparations to electrophoresis in polyacrylamide gels under nondenaturing and denaturing conditions. The chemical composition was principally protein (67.2%), and also comigrating nonessential carbohydrate (10–35%). The physical properties of purified syringacin W-1 were a sedimentation coefficient of 104 for rod-shaped particles, pH stability of 5.2–8.2, and temperature stability from −20 to 40 °C. The bacteriocin was resistant to proteases and to 12 of 13 surfactants tested.

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