Polyamines and acetylpolyamines increase the stability and alter the conformation of nucleosome core particles

Abstract

The interactions of spermine (4+ charge at physiological pH), N1-acetylspermine(3+), spermidine(3+), N1- and N8-acetylsperimidine(2+), putrescine(2+), hexaamminecobalt(3+), and magnesium(2+) with nucleosome core particles have been examined by using thermal denaturation and circular dichroism. Tetra- and triamines were 2-3 times more effective than diamines at stabilizing core particles against thermal denaturation. Secondary effects were also observed, with acetylpolyamines slightly less effective than unmodified polyamines of equivalent charge. Hexaamminecobalt(3+) was less effective than the triamines, while magnesium had essentially no effect. This is surprising since magnesium is more effective than diamines at stabilizing naked DNA. All the cations tested altered the circular dichroism spectra of the core particles in the DNA region (284 nm). The peak at 284 nm was suppressed by tetra- and trivalent compounds to approximately twice the extent of divalent compounds. Magnesium appears to suppress the peak by a lesser extent than the diamines. This indicates that the DNA twist and/or folding is changed by these cations. A plateau of both thermal denaturation and circular dichroism effects was observed at cation concentrations where 30-40% of the total DNA negative charges could be neutralized by the added cations. We suggest that polyamine and histone acetylation function in concert to lower the stability and change the conformation of the nucleosome core, thus facilitating replication and transcription in vivo.

Simian virus 40 minichromosomes as targets for retroviral integration in vivo.

“…3B), although integration into naked SV40 DNA was relatively independent of spermidine. This dependence on spermidine differs from our observations using other minichromosomal targets (8), implying that SV40 minichromosomes may be especially prone to disassembly or rearrangement in the absence of spermidine, which can stabilize nucleosome cores (17). We also tested eight different protocols for preparing SV40 minichromosomes [by varying salt concentrations, divalent cations, lysis procedure, length of SV40 infection, and extent of purification (see ref.…”

NspS, a Predicted Polyamine Sensor, Mediates Activation of Vibrio cholerae Biofilm Formation by Norspermidine

“…They are involved in numerous cellular processes, including the modulation of DNA and RNA functions, protection against oxidative damage, and the regulation of bacterial porins and eukaryotic ion channels (34,37,45,53,78). In this work, we have studied the function of the predicted polyaminebinding protein encoded at locus VC0704.…”

P/CAF-mediated spermidine acetylation regulates histone acetyltransferase activity

“…In Figure 3 Assuming that the increment of P/CAF-HAT activity is not due to spermidine but to N 8 -acetylspermidine, we evaluated its effect on P/CAF-HAT activity measuring initial rates, without (control) and with 0.05-0.8 mM of N 8 -acetylspermidine, holding constant concentrations of acetyl-CoA and histone H3 at 5 and 10 mM, respectively. As shown in Figure 4(A), data plotted as v versus [N 8 -acetylspermidine], that represents enzyme activator, show sigmoid trend. Considering that P/CAF is, however, active in the absence of N 8 -acetylspermidine, it is possible to state that it is a non-essential activator.…”

“…Interestingly, an inverse relationship between the nuclear spermidine N 8 -acetyltransferase and histone acetyltransferase activities was evidenced during the process associated with liver regeneration 11 . Another interesting finding is that APAH, an inhibitor of N 8 -acetylspermidine deacetylase, has been reported to induce a significant increase of L1210 cell growth 12 . In terms of polyamine function in the nucleus, several studies have also implicated polyamines in the formation of high order chromatin fibers.…”

“…Acetylation of spermidine to N 8 -acetylspermidine was first reported with the identification of a nuclear acetyltransferase, highly related to HATs 8 , providing an intriguing link between spermidine metabolism and histone acetylation [8][9][10] . Interestingly, an inverse relationship between the nuclear spermidine N 8 -acetyltransferase and histone acetyltransferase activities was evidenced during the process associated with liver regeneration 11 .…”