DNA-HMGB1 interaction: The nuclear aggregates of polyamine mediation

Native DNA electronics: the Nuclear Aggregates of Polyamines possible role

“…But another important function can be ascribed to these super-aggregates: their interaction with proteins. (15). AFM images clearly show that HMGB1 single molecules assume a pearl necklace configuration, being aligned onto the external wall of the nanotube (Figure 3).…”

“…In the central tract, the DNA is naked and some s-NAP debris, due to the nanotube damage produced, probably, by the cantilever passage, can be perceived (11). 9 and evidenced that NAPs also mediate the interaction of the double strands with HMGB1, a DNA binding protein (10,11,(13)(14)(15)…”

“…AFM image of a Z-DNA tract covered by the m-NAP nanotube, further complexed with HMGB1 proteins (Ternary complexes). These proteins self-dispose in a pearl-lace motif at a few nanometer distance from the strand, so indicating that this space is occupied by the m-NAP nanotube (15).…”

“…Therefore, a role of electronics in DNA physiology cannot be acknowledged, if one limits its consideration to the setting of the bases. On the other hand, another "aromatic" environment is present onto the strands: in native conditions, they are enveloped by a polymeric system of nanotubes formed by the self-assembly of polyamines and phosphate in cyclic structures -the Nuclear Aggregates of Polyamines (NAPs) (6)(7)(8)(9)(10)(11)(12)(13)(14)(15) -that I suggest here as a powerful electronic apparatus that assists the DNA in its functions. This paper has the aim of interpreting the ascertained morphological and functional characteristics of NAPs at the light of the basic principles of the electronics, and hence to 4 delineate their possible role as electronic structures acting in still debated fields of cell nucleus physiology.…”

“…The biochemical structure and the binding forces involved in NAPs system seems to fit well with the factors regulating the messenger proteins motion in the cytosol (33,34). As can be evinced by HMGB1 behavior (15), the interaction of protein with a phosphorous dominion (the external NAP surface) and a guiding EF (assured by the NAP semiconductor device) can be the principal dynamic factors at play in the nucleus also. Theoretically, the efficiency of a possible motive apparatus should be also greater around the strands than in the cytoplasm: in fact, while for cytosol proteins the run happens in the three dimensions (34), in the nucleus, the DNA-binding proteins could be guided by the NAP phosphate-phosphate track (13)(14)(15), so having a strictly predetermined, finalized and efficient motion.…”