| Literature DB >> 1575676 |
A R Slabas1, D Chase, I Nishida, N Murata, C Sidebottom, R Safford, P S Sheldon, R G Kekwick, D G Hardie, R W Mackintosh.
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.Entities:
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Year: 1992 PMID: 1575676 PMCID: PMC1131036 DOI: 10.1042/bj2830321
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857