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. 1992 Apr 15;283(Pt 2):321–326. doi: 10.1042/bj2830321

Molecular cloning of higher-plant 3-oxoacyl-(acyl carrier protein) reductase. Sequence identities with the nodG-gene product of the nitrogen-fixing soil bacterium Rhizobium meliloti.

A R Slabas 1, D Chase 1, I Nishida 1, N Murata 1, C Sidebottom 1, R Safford 1, P S Sheldon 1, R G Kekwick 1, D G Hardie 1, R W Mackintosh 1
PMCID: PMC1131036  PMID: 1575676

Abstract

cDNA clones encoding the fatty-acid- biosynthetic enzyme NADPH-linked 3-oxoacyl-(acyl carrier protein) (ACP) reductase were isolated from a Brassica napus (rape) developing seed library and from an Arabidopsis thaliana (thale cress) leaf library. The N-terminal end of the coding region shows features typical of a stromal-targeting plastid-transit peptide. The deduced amino acid sequences have 41% and 55% identity respectively with the nodG-gene product of Rhizobium meliloti, one of the host-specific genes that restrict infectivity of this bacterium to a small range of host plants. The probability that the nodG-gene product is a oxoreductase strengthens the hypothesis that some of the host-specific nod-gene products are enzymes which synthesize polyketides that uniquely modify the Rhizobium nodulation signal molecule.

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Selected References

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