Abstract Background Horizontal or lateral transfer of genetic material between distantly related prokaryotes has been shown to play a major role in the evolution of bacterial and archaeal genomes, but exchange of genes between prokaryotes and eukaryotes is not as well understood. In particular, gene flow from eukaryotes to prokaryotes is rarely documented with strong support, which is unusual since prokaryotic genomes appear to readily accept foreign genes. Two non-homologous forms of fructose bisphosphate aldolase FBA are characteristic of eukaryotes and prokaryotes respectively. However, a eukaryotic gene has been inserted immediately upstream of the ancestral prokaryotic gene in several strains ecotypes of Synechococcus and Prochlorococcus.
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This article has been cited by other articles in PMC. Abstract The gene encoding the Escherichia coli Class I fructose-1, 6-bisphosphate aldolase FBP aldolase has been cloned and the protein overproduced in high amounts.
This gene sequence has previously been identified as encoding an E. However, the purified protein overproduced from the dhnA gene shares all its properties with those known for the E.
The protein is an mer with a native molecular mass of approx. The active-site peptide has been isolated and the Schiff-base-forming lysine residue Lys has been identified by a combination of site-directed mutagenesis, kinetics and electrospray-ionization MS.
A second lysine residue Lys has been implicated in substrate binding. The cloning of this gene and the high levels of overexpression obtained will facilitate future structure-function studies. Selected References These references are in PubMed. This may not be the complete list of references from this article. Perham RN. The fructose-1,6-bisphosphate aldolases: same reaction, different enzymes.
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Fructose-bisphosphate aldolases: an evolutionary history
This article has been cited by other articles in PMC. Abstract The gene encoding the Escherichia coli Class I fructose-1, 6-bisphosphate aldolase FBP aldolase has been cloned and the protein overproduced in high amounts. This gene sequence has previously been identified as encoding an E. However, the purified protein overproduced from the dhnA gene shares all its properties with those known for the E. The protein is an mer with a native molecular mass of approx. The active-site peptide has been isolated and the Schiff-base-forming lysine residue Lys has been identified by a combination of site-directed mutagenesis, kinetics and electrospray-ionization MS.
Horizontal transfer of a eukaryotic plastid-targeted protein gene to cyanobacteria
This article has been cited by other articles in PMC. Abstract Fructose 1,6-bisphosphate aldolase catalyzes the reversible cleavage of fructose 1,6-bisphosphate and fructose 1-phosphate to dihydroxyacetone phosphate and either glyceraldehyde 3-phosphate or glyceraldehyde, respectively. The existing apo-enzyme structure was refined using the crystallographic free-R-factor and maximum likelihood methods that have been shown to give improved structural results that are less subject to model bias. Crystals were also soaked with the natural substrate fructose 1,6-bisphosphate , and the crystal structure of this complex has been determined to 2. The apo structure differs from the previous Brookhaven-deposited structure 1ald in the flexible C-terminal region.