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P. syringae

There are two pathways for the degradation of nitriles (a) direct formation of carboxylic acids by the activity of a nitrilase, for example, in Bacillus sp. strain OxB-1 and P. syringae B728a (b) hydration to amides followed by hydrolysis, for example, in P. chlororaphis (Oinuma et al. 2003). The monomer acrylonitrile occurs in wastewater from the production of polyacrylonitrile (PAN), and is hydrolyzed by bacteria to acrylate by the combined activity of a nitrilase (hydratase) and an amidase. Acrylate is then degraded by hydration to either lactate or P-hydroxypropionate. The nitrilase or amidase is also capable of hydrolyzing the nitrile group in a number of other nitriles (Robertson et al. 2004) including PAN (Tauber et al. 2000). [Pg.322]

Recent studies have further examined the iron stress response of pseudomonads using an iron-regulated, ice-nucleation gene reporter (inaZ) for induction of the iron stress response (17,18,84). This particular reporter system was developed by Loper and Lindow (85) for study of microbial iron stress on plant surfaces but was later employed in soil assays. In initial. studies, cells of Pseudomonas fluorescens and P. syringae that contained the pvd-inaZ fusion were shown to express iron-responsive ice-nucleation activity in the bean rhizosphere and phyllosphere. Addition of iron to leaves or soil reduced the apparent transcription of the pvd-inaZ reporter gene, as shown by a reduction in the number of ice nuclei produced. [Pg.240]

Mullen et al. (1989) reported that Bacillus cereus, B. subtilis, E. coli and P. aeruginosa were able to sorb an average of 89% of the total Ag+ and 12-27% of the total Cd2+, Cu2+ and La3+ from a ImM solution. Using polyacrylamide-entrapped cells of Brevibacterium sp strain PBZ, Simine et al. (1998) measured a sorption capacity of 40 mg g-1 and 13 mg g-1 dry biomass for Pb and Cd, respectively. Hall et al. (2001) isolated two bacterial strains of P. syringae that were tolerant to 1000 mg L-1 Cu. Similarly, Amoroso et al. (2001) were able to obtain Streptomyces spp. strains R22 and R25 with a high tolerance to Cr from sediments of the Sail River, Argentina. The cells of R22 and R25 could accumulate 10.0 and 5.6 mg Cr g-1 dry weight, respectively, from a concentration of 50 mg Cr mL 1. Cell fractionation studies with strain R22 showed that most of the chromium... [Pg.79]

Hall et al. (2001) measured the biosorption of copper by P. syringae, fitting the experimental data to the Freundlich, Brunauer-Emmett-Teller (BET), and Langmuir equations. Meaningful maximum sorption capacities... [Pg.81]

This group comprises condensation products of salicylic acid with cysteine giving a thiazoline ring. For a review, see (570). Some structurally related compounds will also be mentioned here. Salicylic acid isolated from Burkholderia Pseudomonas) cepacia was named azurochelin (555). It was found to act as a siderophore, e.g. for Pseudomonas fluorescens (230) and P. syringae (178) see also Mycobacterium smegmatis (Sect. 2.8). For details on the siderophore activity of salicylic acid, see (559). [Pg.35]

Accompanied by a non-cyclic pyoverdin with the same amino acid sequence For this pyoverdin an e-amino Lys linkage was claimed but not substantiated. It is probably identical with the pyoverdin from P. putida 9AW where a a-amino Lys linkage was established P. aptata is a pathovar of P. syringae. The same pyoverdin was found produced by P. fluorescens SB83 (20). The identification of P. aptata may, therefore, be questioned (cf. also (179))... [Pg.50]

Some plant pathogenic bacteria and their phytotoxins have been screened in bioassays that monitor the effects of their toxins (antibiotic and phytotoxic) on other sensitive bacteria. For example, several fluorescent Pseudomonas syringae pvs. produce extracellular phytotoxins.76,106,116 Tabtoxin is produced by P. syringae pv. tabaci and pv. coronafacines, and this natural product inhibits glutamine synthetase.34,46,116 Phaseolotoxin, produced by P. syringae pv. phaseolicola... [Pg.342]

Enzyme inhibition can be reversed by supplementation of arginine or citrulline.34 106 Pathovars of P. syringae were shown to inhibit Escherichia coli growth, an effect reversed by L-arginine, but not by L-citrulline or L-glutamine.121 This suggested that the site of action of the toxin produced is involved in the conversion of citrulline to arginine in the urea cycle. [Pg.343]

Pseudomonas is a well studied genus of Pseudomonadaceae. Some species such as P. aeruginosa are pathogens for humans and animals, and some such as P. syringae are plant pathogens. [Pg.131]

Four different avirulence genes have been cloned from P, syringae pv. tomato (70, Shen and Keen, unpublished) that, when... [Pg.122]

In ISR expressing Arabidopsis, it was shown that there are no local and systemic changes in the levels of JA and ET, although an intact response to both JA and ET is required [12,68]. This suggests that ISR is based on an enhanced sensitivity to these plant hormones rather than on an increase in their production. This is supported by ISR expressing plants which show a primed expression of the jasmonate responsive gene Atvsp [22] upon infection with P. syringae pv. tomato. [Pg.105]

As expected, the ascorbate oxidases are very closely related to each other. The bacterial proteins phenoxazinone synthase and the copper resistance gene product from P. syringae are very distant from the other proteins included in Table V. The rape BplO gene product exhibits significant similarity to ascorbate oxidase (about 72% differences). [Pg.154]

Z. Ma, J. J. Zhang, and F. Kong, A concise synthesis of two isomeric pentasaccharides, the O repeat units from the lipopolysaccharides of P. syringae pv. porri NCPPB 3364T and NCPPB 3365, Carbohydr. Res., 339 (2004) 43 -9. [Pg.305]

Translation elongation factors 77.1 23470603 (K)IATDPFVGTLTFVR (K)LAQEDPSFR P. syringae pv. syringae B728a... [Pg.336]


See other pages where P. syringae is mentioned: [Pg.110]    [Pg.111]    [Pg.122]    [Pg.9]    [Pg.375]    [Pg.661]    [Pg.12]    [Pg.83]    [Pg.132]    [Pg.132]    [Pg.374]    [Pg.102]    [Pg.115]    [Pg.115]    [Pg.116]    [Pg.117]    [Pg.117]    [Pg.118]    [Pg.122]    [Pg.122]    [Pg.209]    [Pg.101]    [Pg.101]    [Pg.104]    [Pg.105]    [Pg.1010]    [Pg.145]    [Pg.93]    [Pg.433]    [Pg.16]    [Pg.16]    [Pg.360]    [Pg.360]    [Pg.583]   
See also in sourсe #XX -- [ Pg.79 , Pg.81 ]




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