1995
DOI: 10.1021/bi00008a038 View full text |Buy / Rent full text
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Abstract: A plasmid expression vector, pINSAT2, was constructed in order to express spermidine/spermine N1-acetyltransferase (SSAT) in Escherichia coli. Cells transfected with this vector produced large amounts of SSAT, amounting to up to 2% of the soluble protein when isopropyl beta-D-thiogalactopyranoside (IPTG) was added and 0.3% of the soluble protein in the absence of inducer. The growth rate of cells expressing SSAT was reduced, and all of the cellular spermidine was converted to N1-acetylspermidine, much of which… Show more

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“…Because the induction of human SSAT by polyamine analogs is accompanied by growth inhibition and decreased cell viability of tumor cells, it has been suggested that stress-induced acetylation may occur to specifically inhibit cellular growth (3,27). Furthermore, expression of human SSAT in E. coli results in the conversion of the spermidine to N 1 -acetylspermidine, accompanied by inhibition of exponential growth at 37°C (14,24). However, we have found that in response to spermidine accumulation at low temperature, acetylation occurs to promote exponential growth.…”
Section: Discussionmentioning
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“…Because the induction of human SSAT by polyamine analogs is accompanied by growth inhibition and decreased cell viability of tumor cells, it has been suggested that stress-induced acetylation may occur to specifically inhibit cellular growth (3,27). Furthermore, expression of human SSAT in E. coli results in the conversion of the spermidine to N 1 -acetylspermidine, accompanied by inhibition of exponential growth at 37°C (14,24). However, we have found that in response to spermidine accumulation at low temperature, acetylation occurs to promote exponential growth.…”
Section: Discussionmentioning
“…Acetylation serves to convert the polyamine to a physiologically inert form; acetylpolyamines cannot substitute for polyamines in RNA binding, in the enhancement of growth of an E. coli polyamine-deficient mutant, or in the stimulation of in vitro translation (18). Neither spermidine-deacetylating activity nor polyamine oxidase activity has been detected in E. coli, suggesting that the N-acetylspermidine is either excreted or kept in the inert acetylated form (14,24). SAT is induced under nutrient-poor conditions, and its level is higher in cells growing in minimal medium than in those growing in rich medium (8).…”
mentioning
“…In E. coli, polyamine acetylation is catalyzed by SpeG (4,5,19), and acetylated polyamine is readily excreted (27). E. coli might not recycle acetylated polyamine, and no apparent AphA homologue can be found in this organism as revealed by a BLAST search against all available genome sequences of E. coli strains in the NCBI database.…”
Section: Discussionmentioning
“…Recombinant human SSAT has been efficiently expressed in Escherichia coli using an inducible expression vector (18). In induced cells, all of the cellular spermidine was rapidly converted to the SSAT product, N 1 -acetylspermidine, resulting in a reduction in cellular growth rate (18).…”
mentioning
“…Recombinant human SSAT has been efficiently expressed in Escherichia coli using an inducible expression vector (18). In induced cells, all of the cellular spermidine was rapidly converted to the SSAT product, N 1 -acetylspermidine, resulting in a reduction in cellular growth rate (18). Attempts to constitutively overexpress SSAT in mammalian cells have been unsuccessful due to poor translation of message in the absence of elevated intracellular polyamines (19).…”
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