Rhizosphere bacteria containing 1-aminocyclopropane-1-carboxylate deaminase increase yield of plants grown in drying soil via both local and systemic hormone signalling.

Decreased soil water availability can stimulate production of the plant hormone ethylene and inhibit plant growth. Strategies aimed at decreasing stress ethylene evolution might attenuate its negative effects. An environmentally benign (nonchemical) method of modifying crop ethylene relations - soil inoculation with a natural root-associated bacterium Variovorax paradoxus 5C-2 (containing the enzyme 1-aminocyclopropane-1-carboxylate (ACC) deaminase that degrades the ethylene precursor ACC), was assessed with pea (Pisum sativum) plants grown in drying soil.

Development of a microtiter plate version of the yeast DEL assay amenable to high-throughput toxicity screening of chemical libraries.

The yeast plate-based deletion (DEL) assay has been previously shown to detect a wide range of carcinogens. Of 60 compounds of known carcinogenic activity, 92% were correctly detectable with the DEL assay whereas 62% were correctly detectable with the Ames assay [W.W.

A cathepsin L-like cysteine proteinase gene from the protozoan parasite, Cryptobia salmositica.

The present study describes the identification of a cathepsin L-like cysteine proteinase gene (CYS) from the hemoflagellate Cryptobia salmositica. Genomic DNA sequence of cysteine proteinase was obtained by genome walking using degenerate primers. Specific primers were designed to amplify the cDNA of cysteine proteinase from mRNA by rapid amplification of cDNA ends-PCR.

Reaction mechanisms of the bacterial enzyme 1-aminocyclopropane-1-carboxylate deaminase.

The enzyme 1-aminocyclopropane-1-carboxylate (ACC) deaminase promotes plant growth by sequestering and cleaving plant-produced ACC thereby lowering the level of ethylene in the plant. Decreased ethylene levels allow the plant to be more resistant to a wide variety of environmental stresses. Here the biochemical reaction mechanisms involved in ACC deaminase activity are critically reviewed.

Expression and characterization of 1-aminocyclopropane-1-carboxylate deaminase from the rhizobacterium Pseudomonas putida UW4: a key enzyme in bacterial plant growth promotion.

The enzyme 1-aminocyclopropane-1-carboxylate deaminase (ACCD) converts ACC, the precursor of the plant hormone ethylene, to alpha-ketobutyrate and ammonium. This enzyme has been identified in soil bacteria and has been proposed to play a key role in microbe-plant association. A soluble recombinant ACCD from Pseudomonas putida UW4 of molecular weight 41 kDa has been cloned, expressed, and purified.

Changes in gene expression in canola roots induced by ACC-deaminase-containing plant-growth-promoting bacteria.

The technique of RNA arbitrarily primed-polymerase chain reaction (RAP-PCR) was used to study changes in gene expression over time in canola roots treated with the 1-aminocyclopropane-1-carboxylate (ACC) deaminase-containing plant-growth-promoting bacterium Enterobacter cloacae UW4 and to compare the changes with those in a mutant of E. cloacae UW4 in which the ACC deaminase structural gene acdS was replaced by homologous recombination with acdS with an intentional knockout containing a tetracycline resistance gene. Genes that were either up- or down-regulated over a three-day period in canola plants treated with wild-type or mutant bacteria were isolated, cloned, and sequenced; all appeared to have high homology with Arabidopsis thaliana genes.