Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2051882 | FEBS Letters | 2007 | 6 Pages |
Abstract
In Azotobacter vinelandii the rhdA gene codes for a protein (RhdA) of the rhodanese-homology superfamily. By combining proteomics, enzymic profiles and ultrastructural observations, the phenotype of an A. vinelandii rhdA mutant was analyzed. We found that the A. vinelandii rhdA mutant, and not the wild-type strain, accumulated polyhydroxybutyrate. RhdA deficiency enhanced the expression of enzymes of the polyhydroxybutyrate biosynthetic operon, and affected the activity of specific tricarboxylic acid cycle enzymes. The effect was dramatic on aconitase, in spite of comparable expression of aconitase polypeptides in both strains. By using a model system, we found that RhdA triggered protection from oxidants.
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Authors
Angelo Cereda, Aristodemo Carpen, Gianluca Picariello, Marcello Iriti, Franco Faoro, Pasquale Ferranti, Silvia Pagani,