A Group of Chromosomal Proteins Is Specifically Released by Spermine and Loses DNA-Binding Activity upon Phosphorylation

Abstract

Biologically relevant concentrations as low as 500 PM spermine led to the specific release of chromatin-associated proteins from nuclei of rice (Oryza sativa) seedlings. Using a southwestern technique, it was shown that several of these proteins bind DNA. This affinity was lost upon in organello phosphorylation by an endogenous kinase. The effect of spermine was very specific. Spermidine was far less effective and putrescine was essentially ineffective in releasing these proteins. The most abundant spermine-released protein was shown to be homologous to the maize HMC1 protein.Our results suggest that spermine induces the release of sperminereleased proteins by changing DNA conformation. Binding of these proteins might be sensitive to long-range changes in chromosome structure caused by torsional stress.

Biochemical activity of di- and polyamines in the green alga Chlorella vulgaris Beijerinck (Chlorophyceae)

“…It is well known that the physiological-biochemical activity of di-and polyamines is mainly due to their polycation structure. In all probability, the more number of amine groups in poliamine, the more metabolically active this compound is, because in this way it possesses greater biochemical possibilities to interact with nucleic acids, proteins, hormones and another metabolites characterised by regulating function (Van den Broeck et al 1994;Davis 1997;Tiburcio et al 1997;Laitinen et al 1998;Desideiro et al 1999;Kotzabasis et al 1999). From the studies carried out on the C. vulgaris it was seen that the highest biological activity of spermidine results from the fact that it contains three amine groups of a cation character whereas the lowest activity is noted in agmatine with only one -NH 2 group.…”

“…A few reports (Smith 1985;Dureja-Munjal et al 1992; Van den Broeck et al 1994;Ye et al 1994;Ponappa and Miller 1996;Bagni 1997) showed that di-and polyamines activate the synthesis of secondary cellular signal transmitters, e.g. triphosphoinositol and diacylglycerol mainly by stimulating the synthesis of their direct precursors, the phosphoinositides.…”

“…This is of great importance in the regulation of numerous metabolic transformations, whose mechanism of action consists in phosphorylation and dephosphorylation of specific cellular proteins and lipids. PA stabilize the cell membranous structures and their function, as well, as inhibit ethylene and abscisic acid synthesis (Smith 1985;Scoccianti et al 1989;Bothma and Dubery 1991;Dureja-Munjal 1992;Van den Broeck et al 1994;Ye et al 1994).…”

HMGB1 in health and disease

“…Compared with the single HMGB-box, DNA binding is enhanced when the two domains are covalently connected (A+B) in vitro (Reddy et al, 2005; Stros, 1998, 2001; Yoshioka et al, 1999). Binding of HMGB1 to DNA is also regulated by post-translational modifications (e.g., phosphorylation, acetylation, and oxidization) (Assenberg et al, 2008), pH, ions (e.g., calcium and Mg 2+ ) (Makiguchi et al, 1984; Stros et al, 1990) and the presence of another cationic factor, spermine (Van den Broeck et al, 1994). pH affects interactions between DNA and high-mobility group protein HMG1 (Kohlstaedt and Cole, 1994a).…”

Four differently chromatin‐associated maize HMG domain proteins modulate DNA structure and act as architectural elements in nucleoprotein complexes

“…lanes 1 and 4), much smaller proportions of HMGc and HMGd (Ͻ25%) were extracted (lanes 8 and 12). Accordingly, a protein similar to maize HMGa had been reported to be specifically extracted from rice chromatin by spermine ( Van den Boeck et al, 1994). The molecular mechanism(s) responsible for the specific extraction of HMGa (compared with the structurally similar HMGc and HMGd) by spermine remains to be established.…”