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Background  FabG is the only known enzyme that catalyzes reduction of the 3-ketoacyl-ACP intermediates of bacterial fatty acid synthetic pathways. However, there are two  Ralstonia solanacearum  genes, RSc1052 ( fabG1 ) and RSp0359 ( fabG2 ), annotated as encoding putative 3-ketoacyl-ACP reductases. Both FabG homologues possess the conserved catalytic triad and the N-terminal cofactor binding sequence of the short chain dehydrogenase/reductase (SDR) family. Thus, it seems reasonable to hypothesize that  RsfabG1  and  RsfabG2  both encode functional 3-ketoacyl-ACP reductases and play important roles in  R. solanacearum  fatty acid synthesis and growth.    Methods  Complementation of  Escherichia coli  fabG  temperature-sensitive mutant with  R. solanacearum fabGs  encoded plasmids was carried out to test the function of  RsfabGs  in fatty acid biosynthesis. RsFabGs proteins were purified by nickel chelate chromatography and fatty acid biosynthetic reaction was reconstituted to investigate the 3-ketoacyl-ACP reductase activity of RsFabGs  in vitro . Disruption of both  RsfabG  genes was done via DNA homologous recombination to test the function of both  RsfabG in vivo . And more we also carried out pathogenicity tests on tomato plants using RsfabG mutant strains.     Results  We report that expression of either of the two proteins (RsFabG1 and RsFabG2) restores growth of the  E. coli  fabG temperature-sensitive mutant CL104 under non-permissive conditions.  In vitro  assays demonstrate that both proteins restore fatty acid synthetic ability to extracts of the  E. coli  strain. The  RsfabG1  gene carried on the  R. solanacearum  chromosome is essential for growth of the bacterium, as is the case for  fabG  in  E. coli . In contrast, the null mutant strain with the megaplasmid-encoded  RsfabG2  gene is viable but has a fatty acid composition that differs significantly from that of the wild type strain. Our study also shows that RsFabG2 plays a role in adaptation to high salt concentration and low pH, and in pathogenesis of disease in tomato plants.    Conclusion   R. solanacearum  encodes two 3-ketoacyl-ACP reductases that both have functions in fatty acid synthesis. We supply the first evidence that, like other enzymes in the bacterial fatty acid biosynthetic pathway, one bacterium may simultaneously possess two or more 3-oxoacyl-ACP reductase isozymes.    Electronic supplementary material  The online version of this article (doi:10.1186/s12866-015-0554-x) contains supplementary material, which is available to authorized users.

bmc microbiology

Ralstonia solanacearum fatty acid composition is determined by interaction of two 3-ketoacyl-acyl carrier protein reductases encoded on separate replicons